Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins
The myelin‐derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain. These cell‐surface proteins signal through multi‐subunit neuronal receptors that contain a common ligand‐binding glycosylphosphatidylinositol‐anchored subunit termed the Nogo‐66 recept...
Gespeichert in:
| Veröffentlicht in: | EMBO Journal 2003-07, Vol.22 (13), p.3291-3302 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3302 |
|---|---|
| container_issue | 13 |
| container_start_page | 3291 |
| container_title | EMBO Journal |
| container_volume | 22 |
| creator | Barton, William A. Liu, Betty P. Tzvetkova, Dorothea Jeffrey, Philip D. Fournier, Alyson E. Sah, Dinah Cate, Richard Strittmatter, Stephen M. Nikolov, Dimitar B. |
| description | The myelin‐derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain. These cell‐surface proteins signal through multi‐subunit neuronal receptors that contain a common ligand‐binding glycosylphosphatidylinositol‐anchored subunit termed the Nogo‐66 receptor (NgR). By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell‐surface NgR requires the entire leucine‐rich repeat (LRR) region of NgR, but not other portions of the protein. Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR. To investigate NgR specificity and multi‐ligand binding, we determined the crystal structure of the biologically active ligand‐binding soluble ectodomain of NgR. The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N‐terminal cap and a small C‐terminal subdomain. The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex. |
| doi_str_mv | 10.1093/emboj/cdg325 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_165649</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>18943858</sourcerecordid><originalsourceid>FETCH-LOGICAL-c6535-785c1c4914c7ea40556350622e01adad27d279744b2006db3a8a337a3da764b93</originalsourceid><addsrcrecordid>eNqFkktv1DAUhSMEokNhxxpFILEi1I5f8YIFrdoCKoMQoC5YWI5zJ-MhYw-208e_x0NGpSAEkiUv7nfOfRbFY4xeYiTJAaxbvzowXU9qdqeYYcpRVSPB7hYzVHNcUdzIveJBjCuEEGsEvl_s4bohUko8K75-SmE0aQxQateV-sq70o-pD_4yLUvrlra1yYeyta6zri_9okxLKOe-9xXnZQADm218Kw4w6ARduQk-gXXxYXFvoYcIj3b_fvHl5Pjz0Zvq7MPp26PXZ5XhjLBKNMxgQyWmRoCmiDFOGOJ1DQjrTne1yE8KStsaId61RDeaEKFJpwWnrST7xavJdzO2a-gMuBT0oDbBrnW4Vl5b9XvE2aXq_YXCnHG61T-b9D4mq6KxCczSeOfAJIUZQg2XJFPPd1mC_z5CTGpto4Fh0A78GJUglEiB2H_BvA9KGtZk8Okf4MqPweVRKSxZzWS2y9CLCTLBxxhgcdMXRmp7AOrnAajpADL-5PYsfsG7jWeATcClHeD6n2bq-P3hO8FyKWRrXE26mCWuh3Cr2L8XsuNtTHB1k0eHb4oLIpg6n58qfEjQx7lo1Dn5AcdW3Ms</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>195259970</pqid></control><display><type>article</type><title>Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Wiley Online Library Free Content</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Barton, William A. ; Liu, Betty P. ; Tzvetkova, Dorothea ; Jeffrey, Philip D. ; Fournier, Alyson E. ; Sah, Dinah ; Cate, Richard ; Strittmatter, Stephen M. ; Nikolov, Dimitar B.</creator><creatorcontrib>Barton, William A. ; Liu, Betty P. ; Tzvetkova, Dorothea ; Jeffrey, Philip D. ; Fournier, Alyson E. ; Sah, Dinah ; Cate, Richard ; Strittmatter, Stephen M. ; Nikolov, Dimitar B. ; Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><description>The myelin‐derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain. These cell‐surface proteins signal through multi‐subunit neuronal receptors that contain a common ligand‐binding glycosylphosphatidylinositol‐anchored subunit termed the Nogo‐66 receptor (NgR). By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell‐surface NgR requires the entire leucine‐rich repeat (LRR) region of NgR, but not other portions of the protein. Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR. To investigate NgR specificity and multi‐ligand binding, we determined the crystal structure of the biologically active ligand‐binding soluble ectodomain of NgR. The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N‐terminal cap and a small C‐terminal subdomain. The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/cdg325</identifier><identifier>PMID: 12839991</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Animals ; axon outgrowth ; Axons ; BASIC BIOLOGICAL SCIENCES ; CHEMICAL BONDS ; Crystallization ; EMBO27 ; EMBO40 ; GPI-Linked Proteins ; INHIBITION ; leucine-rich repeats ; ligand binding ; Mice ; Models, Molecular ; Molecular Sequence Data ; Myelin Proteins - chemistry ; Myelin Proteins - metabolism ; NATIONAL SYNCHROTRON LIGHT SOURCE ; NERVE CELLS ; Nogo protein ; Nogo Receptor 1 ; Nogo-66 receptor ; Protein Binding ; Protein Conformation ; PROTEIN STRUCTURE ; Proteins ; RECEPTORS ; Receptors, Cell Surface - chemistry ; Receptors, Cell Surface - metabolism ; Sequence Homology, Amino Acid</subject><ispartof>EMBO Journal, 2003-07, Vol.22 (13), p.3291-3302</ispartof><rights>European Molecular Biology Organization 2003</rights><rights>Copyright © 2003 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Jul 1, 2003</rights><rights>Copyright © 2003 European Molecular Biology Organization 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6535-785c1c4914c7ea40556350622e01adad27d279744b2006db3a8a337a3da764b93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC165649/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC165649/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12839991$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/15008693$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Barton, William A.</creatorcontrib><creatorcontrib>Liu, Betty P.</creatorcontrib><creatorcontrib>Tzvetkova, Dorothea</creatorcontrib><creatorcontrib>Jeffrey, Philip D.</creatorcontrib><creatorcontrib>Fournier, Alyson E.</creatorcontrib><creatorcontrib>Sah, Dinah</creatorcontrib><creatorcontrib>Cate, Richard</creatorcontrib><creatorcontrib>Strittmatter, Stephen M.</creatorcontrib><creatorcontrib>Nikolov, Dimitar B.</creatorcontrib><creatorcontrib>Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><title>Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins</title><title>EMBO Journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>The myelin‐derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain. These cell‐surface proteins signal through multi‐subunit neuronal receptors that contain a common ligand‐binding glycosylphosphatidylinositol‐anchored subunit termed the Nogo‐66 receptor (NgR). By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell‐surface NgR requires the entire leucine‐rich repeat (LRR) region of NgR, but not other portions of the protein. Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR. To investigate NgR specificity and multi‐ligand binding, we determined the crystal structure of the biologically active ligand‐binding soluble ectodomain of NgR. The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N‐terminal cap and a small C‐terminal subdomain. The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>axon outgrowth</subject><subject>Axons</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>CHEMICAL BONDS</subject><subject>Crystallization</subject><subject>EMBO27</subject><subject>EMBO40</subject><subject>GPI-Linked Proteins</subject><subject>INHIBITION</subject><subject>leucine-rich repeats</subject><subject>ligand binding</subject><subject>Mice</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Myelin Proteins - chemistry</subject><subject>Myelin Proteins - metabolism</subject><subject>NATIONAL SYNCHROTRON LIGHT SOURCE</subject><subject>NERVE CELLS</subject><subject>Nogo protein</subject><subject>Nogo Receptor 1</subject><subject>Nogo-66 receptor</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>PROTEIN STRUCTURE</subject><subject>Proteins</subject><subject>RECEPTORS</subject><subject>Receptors, Cell Surface - chemistry</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkktv1DAUhSMEokNhxxpFILEi1I5f8YIFrdoCKoMQoC5YWI5zJ-MhYw-208e_x0NGpSAEkiUv7nfOfRbFY4xeYiTJAaxbvzowXU9qdqeYYcpRVSPB7hYzVHNcUdzIveJBjCuEEGsEvl_s4bohUko8K75-SmE0aQxQateV-sq70o-pD_4yLUvrlra1yYeyta6zri_9okxLKOe-9xXnZQADm218Kw4w6ARduQk-gXXxYXFvoYcIj3b_fvHl5Pjz0Zvq7MPp26PXZ5XhjLBKNMxgQyWmRoCmiDFOGOJ1DQjrTne1yE8KStsaId61RDeaEKFJpwWnrST7xavJdzO2a-gMuBT0oDbBrnW4Vl5b9XvE2aXq_YXCnHG61T-b9D4mq6KxCczSeOfAJIUZQg2XJFPPd1mC_z5CTGpto4Fh0A78GJUglEiB2H_BvA9KGtZk8Okf4MqPweVRKSxZzWS2y9CLCTLBxxhgcdMXRmp7AOrnAajpADL-5PYsfsG7jWeATcClHeD6n2bq-P3hO8FyKWRrXE26mCWuh3Cr2L8XsuNtTHB1k0eHb4oLIpg6n58qfEjQx7lo1Dn5AcdW3Ms</recordid><startdate>20030701</startdate><enddate>20030701</enddate><creator>Barton, William A.</creator><creator>Liu, Betty P.</creator><creator>Tzvetkova, Dorothea</creator><creator>Jeffrey, Philip D.</creator><creator>Fournier, Alyson E.</creator><creator>Sah, Dinah</creator><creator>Cate, Richard</creator><creator>Strittmatter, Stephen M.</creator><creator>Nikolov, Dimitar B.</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><general>Oxford University Press</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20030701</creationdate><title>Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins</title><author>Barton, William A. ; Liu, Betty P. ; Tzvetkova, Dorothea ; Jeffrey, Philip D. ; Fournier, Alyson E. ; Sah, Dinah ; Cate, Richard ; Strittmatter, Stephen M. ; Nikolov, Dimitar B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6535-785c1c4914c7ea40556350622e01adad27d279744b2006db3a8a337a3da764b93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>axon outgrowth</topic><topic>Axons</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>CHEMICAL BONDS</topic><topic>Crystallization</topic><topic>EMBO27</topic><topic>EMBO40</topic><topic>GPI-Linked Proteins</topic><topic>INHIBITION</topic><topic>leucine-rich repeats</topic><topic>ligand binding</topic><topic>Mice</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Myelin Proteins - chemistry</topic><topic>Myelin Proteins - metabolism</topic><topic>NATIONAL SYNCHROTRON LIGHT SOURCE</topic><topic>NERVE CELLS</topic><topic>Nogo protein</topic><topic>Nogo Receptor 1</topic><topic>Nogo-66 receptor</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>PROTEIN STRUCTURE</topic><topic>Proteins</topic><topic>RECEPTORS</topic><topic>Receptors, Cell Surface - chemistry</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Barton, William A.</creatorcontrib><creatorcontrib>Liu, Betty P.</creatorcontrib><creatorcontrib>Tzvetkova, Dorothea</creatorcontrib><creatorcontrib>Jeffrey, Philip D.</creatorcontrib><creatorcontrib>Fournier, Alyson E.</creatorcontrib><creatorcontrib>Sah, Dinah</creatorcontrib><creatorcontrib>Cate, Richard</creatorcontrib><creatorcontrib>Strittmatter, Stephen M.</creatorcontrib><creatorcontrib>Nikolov, Dimitar B.</creatorcontrib><creatorcontrib>Brookhaven National Laboratory, National Synchrotron Light Source (US)</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO Journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Barton, William A.</au><au>Liu, Betty P.</au><au>Tzvetkova, Dorothea</au><au>Jeffrey, Philip D.</au><au>Fournier, Alyson E.</au><au>Sah, Dinah</au><au>Cate, Richard</au><au>Strittmatter, Stephen M.</au><au>Nikolov, Dimitar B.</au><aucorp>Brookhaven National Laboratory, National Synchrotron Light Source (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins</atitle><jtitle>EMBO Journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2003-07-01</date><risdate>2003</risdate><volume>22</volume><issue>13</issue><spage>3291</spage><epage>3302</epage><pages>3291-3302</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>The myelin‐derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain. These cell‐surface proteins signal through multi‐subunit neuronal receptors that contain a common ligand‐binding glycosylphosphatidylinositol‐anchored subunit termed the Nogo‐66 receptor (NgR). By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell‐surface NgR requires the entire leucine‐rich repeat (LRR) region of NgR, but not other portions of the protein. Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR. To investigate NgR specificity and multi‐ligand binding, we determined the crystal structure of the biologically active ligand‐binding soluble ectodomain of NgR. The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N‐terminal cap and a small C‐terminal subdomain. The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12839991</pmid><doi>10.1093/emboj/cdg325</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0261-4189 |
| ispartof | EMBO Journal, 2003-07, Vol.22 (13), p.3291-3302 |
| issn | 0261-4189 1460-2075 1460-2075 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_165649 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Animals axon outgrowth Axons BASIC BIOLOGICAL SCIENCES CHEMICAL BONDS Crystallization EMBO27 EMBO40 GPI-Linked Proteins INHIBITION leucine-rich repeats ligand binding Mice Models, Molecular Molecular Sequence Data Myelin Proteins - chemistry Myelin Proteins - metabolism NATIONAL SYNCHROTRON LIGHT SOURCE NERVE CELLS Nogo protein Nogo Receptor 1 Nogo-66 receptor Protein Binding Protein Conformation PROTEIN STRUCTURE Proteins RECEPTORS Receptors, Cell Surface - chemistry Receptors, Cell Surface - metabolism Sequence Homology, Amino Acid |
| title | Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T15%3A22%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structure%20and%20axon%20outgrowth%20inhibitor%20binding%20of%20the%20Nogo-66%20receptor%20and%20related%20proteins&rft.jtitle=EMBO%20Journal&rft.au=Barton,%20William%20A.&rft.aucorp=Brookhaven%20National%20Laboratory,%20National%20Synchrotron%20Light%20Source%20(US)&rft.date=2003-07-01&rft.volume=22&rft.issue=13&rft.spage=3291&rft.epage=3302&rft.pages=3291-3302&rft.issn=0261-4189&rft.eissn=1460-2075&rft.coden=EMJODG&rft_id=info:doi/10.1093/emboj/cdg325&rft_dat=%3Cproquest_pubme%3E18943858%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=195259970&rft_id=info:pmid/12839991&rfr_iscdi=true |