Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)
Human islet amyloid polypeptide (IAPP or amylin) is a 37‐residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we ha...
Gespeichert in:
| Veröffentlicht in: | Protein science 2008-09, Vol.17 (9), p.1467-1474 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1474 |
|---|---|
| container_issue | 9 |
| container_start_page | 1467 |
| container_title | Protein science |
| container_volume | 17 |
| creator | Wiltzius, Jed J.W. Sievers, Stuart A. Sawaya, Michael R. Cascio, Duilio Popov, Dmitriy Riekel, Christian Eisenberg, David |
| description | Human islet amyloid polypeptide (IAPP or amylin) is a 37‐residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid‐like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full‐length IAPP polymorph. |
| doi_str_mv | 10.1110/ps.036509.108 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2525530</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>69462081</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4287-4c95e86afb7b14ca0bbb8e30fffa0973d4ea036e3f29db1204e914c8db88b2243</originalsourceid><addsrcrecordid>eNp9kclKxTAUhoMoeh2WbqUr0UWvmZomG0HECURFFNyFpD3VSNvUplXuzkfwWXwQH8InsXovDhtXB_7z8Z_hR2id4DEhBO80YYyZSLAaEyzn0IhwoWKpxM08GmElSCyZkEtoOYR7jDEnlC2iJSKTRPCUjdDZXucrl0Wha_us61uIfBF1dxBlrQ_h_fnl7TUKjau_dBdK6CJTTUrv8qjx5aSBpnM5RFufoqu3V9FCYcoAa7O6gq4PD672j-PT86OT_b3TOONUpjHPVAJSmMKmlvDMYGutBIaLojBYpSznYIargBVU5ZZQzEENnMytlJZSzlbQ7tS36W0FeQZ115pSN62rTDvR3jj9t1O7O33rHzVNaJIwPBhszgxa_9BD6HTlQgZlaWrwfdBCcUGxJAMYT8Gvh7RQfA8hWH8moJugpwkMihz4jd-b_dCzlw8AnQJProTJ_2764vJ8CDRlH_e1lK8</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69462081</pqid></control><display><type>article</type><title>Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)</title><source>Wiley Free Content</source><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Wiltzius, Jed J.W. ; Sievers, Stuart A. ; Sawaya, Michael R. ; Cascio, Duilio ; Popov, Dmitriy ; Riekel, Christian ; Eisenberg, David</creator><creatorcontrib>Wiltzius, Jed J.W. ; Sievers, Stuart A. ; Sawaya, Michael R. ; Cascio, Duilio ; Popov, Dmitriy ; Riekel, Christian ; Eisenberg, David</creatorcontrib><description>Human islet amyloid polypeptide (IAPP or amylin) is a 37‐residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid‐like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full‐length IAPP polymorph.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1110/ps.036509.108</identifier><identifier>PMID: 18556473</identifier><language>eng</language><publisher>Bristol: Cold Spring Harbor Laboratory Press</publisher><subject>Accelerated Communication ; aggregation ; Amino Acid Sequence ; amylin ; amyloid ; Amyloid - chemistry ; Amyloid - genetics ; Amyloid - isolation & purification ; Amyloid - metabolism ; Amyloid - ultrastructure ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Computer Simulation ; Crystallization ; Diabetes Mellitus, Type 2 - metabolism ; Diabetes Mellitus, Type 2 - physiopathology ; Disulfides - chemistry ; Histidine - metabolism ; Humans ; Hydrogen Bonding ; IAPP ; Islet Amyloid Polypeptide ; Islets of Langerhans - chemistry ; Maltose-Binding Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; protein crystallization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - metabolism ; Sequence Homology, Amino Acid ; Solubility ; type 2 diabetes ; X-Ray Diffraction</subject><ispartof>Protein science, 2008-09, Vol.17 (9), p.1467-1474</ispartof><rights>Copyright © 2008 The Protein Society</rights><rights>Copyright © 2008 The Protein Society 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4287-4c95e86afb7b14ca0bbb8e30fffa0973d4ea036e3f29db1204e914c8db88b2243</citedby><cites>FETCH-LOGICAL-c4287-4c95e86afb7b14ca0bbb8e30fffa0973d4ea036e3f29db1204e914c8db88b2243</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2525530/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2525530/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27902,27903,45552,45553,46386,46810,53768,53770</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18556473$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wiltzius, Jed J.W.</creatorcontrib><creatorcontrib>Sievers, Stuart A.</creatorcontrib><creatorcontrib>Sawaya, Michael R.</creatorcontrib><creatorcontrib>Cascio, Duilio</creatorcontrib><creatorcontrib>Popov, Dmitriy</creatorcontrib><creatorcontrib>Riekel, Christian</creatorcontrib><creatorcontrib>Eisenberg, David</creatorcontrib><title>Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>Human islet amyloid polypeptide (IAPP or amylin) is a 37‐residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid‐like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full‐length IAPP polymorph.</description><subject>Accelerated Communication</subject><subject>aggregation</subject><subject>Amino Acid Sequence</subject><subject>amylin</subject><subject>amyloid</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - genetics</subject><subject>Amyloid - isolation & purification</subject><subject>Amyloid - metabolism</subject><subject>Amyloid - ultrastructure</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Computer Simulation</subject><subject>Crystallization</subject><subject>Diabetes Mellitus, Type 2 - metabolism</subject><subject>Diabetes Mellitus, Type 2 - physiopathology</subject><subject>Disulfides - chemistry</subject><subject>Histidine - metabolism</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>IAPP</subject><subject>Islet Amyloid Polypeptide</subject><subject>Islets of Langerhans - chemistry</subject><subject>Maltose-Binding Proteins</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Protein Conformation</subject><subject>protein crystallization</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Solubility</subject><subject>type 2 diabetes</subject><subject>X-Ray Diffraction</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kclKxTAUhoMoeh2WbqUr0UWvmZomG0HECURFFNyFpD3VSNvUplXuzkfwWXwQH8InsXovDhtXB_7z8Z_hR2id4DEhBO80YYyZSLAaEyzn0IhwoWKpxM08GmElSCyZkEtoOYR7jDEnlC2iJSKTRPCUjdDZXucrl0Wha_us61uIfBF1dxBlrQ_h_fnl7TUKjau_dBdK6CJTTUrv8qjx5aSBpnM5RFufoqu3V9FCYcoAa7O6gq4PD672j-PT86OT_b3TOONUpjHPVAJSmMKmlvDMYGutBIaLojBYpSznYIargBVU5ZZQzEENnMytlJZSzlbQ7tS36W0FeQZ115pSN62rTDvR3jj9t1O7O33rHzVNaJIwPBhszgxa_9BD6HTlQgZlaWrwfdBCcUGxJAMYT8Gvh7RQfA8hWH8moJugpwkMihz4jd-b_dCzlw8AnQJProTJ_2764vJ8CDRlH_e1lK8</recordid><startdate>200809</startdate><enddate>200809</enddate><creator>Wiltzius, Jed J.W.</creator><creator>Sievers, Stuart A.</creator><creator>Sawaya, Michael R.</creator><creator>Cascio, Duilio</creator><creator>Popov, Dmitriy</creator><creator>Riekel, Christian</creator><creator>Eisenberg, David</creator><general>Cold Spring Harbor Laboratory Press</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>200809</creationdate><title>Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)</title><author>Wiltzius, Jed J.W. ; Sievers, Stuart A. ; Sawaya, Michael R. ; Cascio, Duilio ; Popov, Dmitriy ; Riekel, Christian ; Eisenberg, David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4287-4c95e86afb7b14ca0bbb8e30fffa0973d4ea036e3f29db1204e914c8db88b2243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Accelerated Communication</topic><topic>aggregation</topic><topic>Amino Acid Sequence</topic><topic>amylin</topic><topic>amyloid</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - genetics</topic><topic>Amyloid - isolation & purification</topic><topic>Amyloid - metabolism</topic><topic>Amyloid - ultrastructure</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>Computer Simulation</topic><topic>Crystallization</topic><topic>Diabetes Mellitus, Type 2 - metabolism</topic><topic>Diabetes Mellitus, Type 2 - physiopathology</topic><topic>Disulfides - chemistry</topic><topic>Histidine - metabolism</topic><topic>Humans</topic><topic>Hydrogen Bonding</topic><topic>IAPP</topic><topic>Islet Amyloid Polypeptide</topic><topic>Islets of Langerhans - chemistry</topic><topic>Maltose-Binding Proteins</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Protein Conformation</topic><topic>protein crystallization</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Solubility</topic><topic>type 2 diabetes</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wiltzius, Jed J.W.</creatorcontrib><creatorcontrib>Sievers, Stuart A.</creatorcontrib><creatorcontrib>Sawaya, Michael R.</creatorcontrib><creatorcontrib>Cascio, Duilio</creatorcontrib><creatorcontrib>Popov, Dmitriy</creatorcontrib><creatorcontrib>Riekel, Christian</creatorcontrib><creatorcontrib>Eisenberg, David</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wiltzius, Jed J.W.</au><au>Sievers, Stuart A.</au><au>Sawaya, Michael R.</au><au>Cascio, Duilio</au><au>Popov, Dmitriy</au><au>Riekel, Christian</au><au>Eisenberg, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin)</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2008-09</date><risdate>2008</risdate><volume>17</volume><issue>9</issue><spage>1467</spage><epage>1474</epage><pages>1467-1474</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>Human islet amyloid polypeptide (IAPP or amylin) is a 37‐residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. Although the cellular toxicity of IAPP has been established, the structure of the fibrillar form found in these deposits is unknown. Here we have crystallized two segments from IAPP, which themselves form amyloid‐like fibrils. The atomic structures of these two segments, NNFGAIL and SSTNVG, were determined, and form the basis of a model for the most commonly observed, full‐length IAPP polymorph.</abstract><cop>Bristol</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>18556473</pmid><doi>10.1110/ps.036509.108</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0961-8368 |
| ispartof | Protein science, 2008-09, Vol.17 (9), p.1467-1474 |
| issn | 0961-8368 1469-896X |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2525530 |
| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Accelerated Communication aggregation Amino Acid Sequence amylin amyloid Amyloid - chemistry Amyloid - genetics Amyloid - isolation & purification Amyloid - metabolism Amyloid - ultrastructure Carrier Proteins - chemistry Carrier Proteins - metabolism Computer Simulation Crystallization Diabetes Mellitus, Type 2 - metabolism Diabetes Mellitus, Type 2 - physiopathology Disulfides - chemistry Histidine - metabolism Humans Hydrogen Bonding IAPP Islet Amyloid Polypeptide Islets of Langerhans - chemistry Maltose-Binding Proteins Models, Molecular Molecular Sequence Data Mutation Protein Conformation protein crystallization Protein Structure, Secondary Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Sequence Homology, Amino Acid Solubility type 2 diabetes X-Ray Diffraction |
| title | Atomic structure of the cross‐β spine of islet amyloid polypeptide (amylin) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T08%3A38%3A08IST&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=Atomic%20structure%20of%20the%20cross%E2%80%90%CE%B2%20spine%20of%20islet%20amyloid%20polypeptide%20(amylin)&rft.jtitle=Protein%20science&rft.au=Wiltzius,%20Jed%20J.W.&rft.date=2008-09&rft.volume=17&rft.issue=9&rft.spage=1467&rft.epage=1474&rft.pages=1467-1474&rft.issn=0961-8368&rft.eissn=1469-896X&rft_id=info:doi/10.1110/ps.036509.108&rft_dat=%3Cproquest_pubme%3E69462081%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=69462081&rft_id=info:pmid/18556473&rfr_iscdi=true |