Role of Asp297 of the AT2 receptor in high-affinity binding to different peptide ligands
To determine how ligand-receptor interaction is affected by the charges of the amino acids at position 2 of the ligands and position 297 of the AT2 receptor, we generated the Asp297Lys mutant of AT2 and a ligand SarAsp 2Ile. Asp297Lys mutant lost affinity to Ang II and SarIle however retained partia...
Gespeichert in:
| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2001-12, Vol.22 (12), p.2145-2149 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2149 |
|---|---|
| container_issue | 12 |
| container_start_page | 2145 |
| container_title | Peptides (New York, N.Y. : 1980) |
| container_volume | 22 |
| creator | Knowle, Dieter Kurfis, Jayson Gavini, Narasaiah Pulakat, Lakshmidevi |
| description | To determine how ligand-receptor interaction is affected by the charges of the amino acids at position 2 of the ligands and position 297 of the AT2 receptor, we generated the Asp297Lys mutant of AT2 and a ligand SarAsp
2Ile. Asp297Lys mutant lost affinity to Ang II and SarIle however retained partial affinity to
125I-CGP42112A. The SarAsp
2Ile had high affinity to Asp297Lys (IC
503.5nM) and partial affinity to the AT2 (IC
5015nM). Therefore, not only the charge, but also the length of the side arms of the amino acids at position 2 of the ligand and position 297 of the receptor affect their interaction. |
| doi_str_mv | 10.1016/S0196-9781(01)00553-8 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_72400974</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0196978101005538</els_id><sourcerecordid>72400974</sourcerecordid><originalsourceid>FETCH-LOGICAL-c361t-df3f8866e73015d353d591292c7fbd27a7a876d6df52f19be8fd88faf059cf593</originalsourceid><addsrcrecordid>eNqFkE1Lw0AQhhdRbP34CcqeRA_R3U326ySl-AUFQSt4W5LsbLuSJnE3FfrvTWzRozAwc3jeGeZB6IySa0qouHklVItES0UvCb0ihPM0UXtoTJVME06F3kfjX2SEjmL8IIRkmVaHaESpVIIRNkbvL00FuHF4Elum5TB1S8CTOcMBSmi7JmBf46VfLJPcOV_7boMLX1tfL3DXYOudgwB1h9se9hZw5Rd5beMJOnB5FeF014_R2_3dfPqYzJ4fnqaTWVKmgnaJdalTSgiQKaHcpjy1XFOmWSldYZnMZa6ksMI6zhzVBShnlXK5I1yXjuv0GF1s97ah-VxD7MzKxxKqKq-hWUcjWUaIllkP8i1YhibGAM60wa_ysDGUmEGp-VFqBl-G9DUoNarPne8OrIsV2L_UzmEP3G4B6N_88hBMLD3UJVjfK-yMbfw_J74BguyFMw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>72400974</pqid></control><display><type>article</type><title>Role of Asp297 of the AT2 receptor in high-affinity binding to different peptide ligands</title><source>MEDLINE</source><source>ScienceDirect</source><creator>Knowle, Dieter ; Kurfis, Jayson ; Gavini, Narasaiah ; Pulakat, Lakshmidevi</creator><creatorcontrib>Knowle, Dieter ; Kurfis, Jayson ; Gavini, Narasaiah ; Pulakat, Lakshmidevi</creatorcontrib><description>To determine how ligand-receptor interaction is affected by the charges of the amino acids at position 2 of the ligands and position 297 of the AT2 receptor, we generated the Asp297Lys mutant of AT2 and a ligand SarAsp
2Ile. Asp297Lys mutant lost affinity to Ang II and SarIle however retained partial affinity to
125I-CGP42112A. The SarAsp
2Ile had high affinity to Asp297Lys (IC
503.5nM) and partial affinity to the AT2 (IC
5015nM). Therefore, not only the charge, but also the length of the side arms of the amino acids at position 2 of the ligand and position 297 of the receptor affect their interaction.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/S0196-9781(01)00553-8</identifier><identifier>PMID: 11786202</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Angiotensin II ; Aspartic Acid - metabolism ; AT2 receptor ; Ligands ; Molecular Sequence Data ; Phospholipase C ; Protein Binding ; Receptors, Angiotensin - chemistry ; Receptors, Angiotensin - metabolism ; Third extracellular loop ; Transmembrane domain ; Xenopus oocytes</subject><ispartof>Peptides (New York, N.Y. : 1980), 2001-12, Vol.22 (12), p.2145-2149</ispartof><rights>2002 Elsevier Science Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c361t-df3f8866e73015d353d591292c7fbd27a7a876d6df52f19be8fd88faf059cf593</citedby><cites>FETCH-LOGICAL-c361t-df3f8866e73015d353d591292c7fbd27a7a876d6df52f19be8fd88faf059cf593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0196-9781(01)00553-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11786202$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Knowle, Dieter</creatorcontrib><creatorcontrib>Kurfis, Jayson</creatorcontrib><creatorcontrib>Gavini, Narasaiah</creatorcontrib><creatorcontrib>Pulakat, Lakshmidevi</creatorcontrib><title>Role of Asp297 of the AT2 receptor in high-affinity binding to different peptide ligands</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>To determine how ligand-receptor interaction is affected by the charges of the amino acids at position 2 of the ligands and position 297 of the AT2 receptor, we generated the Asp297Lys mutant of AT2 and a ligand SarAsp
2Ile. Asp297Lys mutant lost affinity to Ang II and SarIle however retained partial affinity to
125I-CGP42112A. The SarAsp
2Ile had high affinity to Asp297Lys (IC
503.5nM) and partial affinity to the AT2 (IC
5015nM). Therefore, not only the charge, but also the length of the side arms of the amino acids at position 2 of the ligand and position 297 of the receptor affect their interaction.</description><subject>Amino Acid Sequence</subject><subject>Angiotensin II</subject><subject>Aspartic Acid - metabolism</subject><subject>AT2 receptor</subject><subject>Ligands</subject><subject>Molecular Sequence Data</subject><subject>Phospholipase C</subject><subject>Protein Binding</subject><subject>Receptors, Angiotensin - chemistry</subject><subject>Receptors, Angiotensin - metabolism</subject><subject>Third extracellular loop</subject><subject>Transmembrane domain</subject><subject>Xenopus oocytes</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AQhhdRbP34CcqeRA_R3U326ySl-AUFQSt4W5LsbLuSJnE3FfrvTWzRozAwc3jeGeZB6IySa0qouHklVItES0UvCb0ihPM0UXtoTJVME06F3kfjX2SEjmL8IIRkmVaHaESpVIIRNkbvL00FuHF4Elum5TB1S8CTOcMBSmi7JmBf46VfLJPcOV_7boMLX1tfL3DXYOudgwB1h9se9hZw5Rd5beMJOnB5FeF014_R2_3dfPqYzJ4fnqaTWVKmgnaJdalTSgiQKaHcpjy1XFOmWSldYZnMZa6ksMI6zhzVBShnlXK5I1yXjuv0GF1s97ah-VxD7MzKxxKqKq-hWUcjWUaIllkP8i1YhibGAM60wa_ysDGUmEGp-VFqBl-G9DUoNarPne8OrIsV2L_UzmEP3G4B6N_88hBMLD3UJVjfK-yMbfw_J74BguyFMw</recordid><startdate>20011201</startdate><enddate>20011201</enddate><creator>Knowle, Dieter</creator><creator>Kurfis, Jayson</creator><creator>Gavini, Narasaiah</creator><creator>Pulakat, Lakshmidevi</creator><general>Elsevier Inc</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></search><sort><creationdate>20011201</creationdate><title>Role of Asp297 of the AT2 receptor in high-affinity binding to different peptide ligands</title><author>Knowle, Dieter ; Kurfis, Jayson ; Gavini, Narasaiah ; Pulakat, Lakshmidevi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c361t-df3f8866e73015d353d591292c7fbd27a7a876d6df52f19be8fd88faf059cf593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Angiotensin II</topic><topic>Aspartic Acid - metabolism</topic><topic>AT2 receptor</topic><topic>Ligands</topic><topic>Molecular Sequence Data</topic><topic>Phospholipase C</topic><topic>Protein Binding</topic><topic>Receptors, Angiotensin - chemistry</topic><topic>Receptors, Angiotensin - metabolism</topic><topic>Third extracellular loop</topic><topic>Transmembrane domain</topic><topic>Xenopus oocytes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Knowle, Dieter</creatorcontrib><creatorcontrib>Kurfis, Jayson</creatorcontrib><creatorcontrib>Gavini, Narasaiah</creatorcontrib><creatorcontrib>Pulakat, Lakshmidevi</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><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Knowle, Dieter</au><au>Kurfis, Jayson</au><au>Gavini, Narasaiah</au><au>Pulakat, Lakshmidevi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Asp297 of the AT2 receptor in high-affinity binding to different peptide ligands</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2001-12-01</date><risdate>2001</risdate><volume>22</volume><issue>12</issue><spage>2145</spage><epage>2149</epage><pages>2145-2149</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><abstract>To determine how ligand-receptor interaction is affected by the charges of the amino acids at position 2 of the ligands and position 297 of the AT2 receptor, we generated the Asp297Lys mutant of AT2 and a ligand SarAsp
2Ile. Asp297Lys mutant lost affinity to Ang II and SarIle however retained partial affinity to
125I-CGP42112A. The SarAsp
2Ile had high affinity to Asp297Lys (IC
503.5nM) and partial affinity to the AT2 (IC
5015nM). Therefore, not only the charge, but also the length of the side arms of the amino acids at position 2 of the ligand and position 297 of the receptor affect their interaction.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11786202</pmid><doi>10.1016/S0196-9781(01)00553-8</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 2001-12, Vol.22 (12), p.2145-2149 |
| issn | 0196-9781 1873-5169 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72400974 |
| source | MEDLINE; ScienceDirect |
| subjects | Amino Acid Sequence Angiotensin II Aspartic Acid - metabolism AT2 receptor Ligands Molecular Sequence Data Phospholipase C Protein Binding Receptors, Angiotensin - chemistry Receptors, Angiotensin - metabolism Third extracellular loop Transmembrane domain Xenopus oocytes |
| title | Role of Asp297 of the AT2 receptor in high-affinity binding to different peptide ligands |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-13T23%3A01%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Role%20of%20Asp297%20of%20the%20AT2%20receptor%20in%20high-affinity%20binding%20to%20different%20peptide%20ligands&rft.jtitle=Peptides%20(New%20York,%20N.Y.%20:%201980)&rft.au=Knowle,%20Dieter&rft.date=2001-12-01&rft.volume=22&rft.issue=12&rft.spage=2145&rft.epage=2149&rft.pages=2145-2149&rft.issn=0196-9781&rft.eissn=1873-5169&rft_id=info:doi/10.1016/S0196-9781(01)00553-8&rft_dat=%3Cproquest_cross%3E72400974%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=72400974&rft_id=info:pmid/11786202&rft_els_id=S0196978101005538&rfr_iscdi=true |