Conopressin-T from Conus tulipa Reveals an Antagonist Switch in Vasopressin-like Peptides
We report the discovery of conopressin-T, a novel bioactive peptide isolated from Conus tulipa venom. Conopressin-T belongs to the vasopressin-like peptide family and displays high sequence homology to the mammalian hormone oxytocin (OT) and to vasotocin, the endogenous vasopressin analogue found in...
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| Veröffentlicht in: | The Journal of biological chemistry 2008-03, Vol.283 (11), p.7100-7108 |
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| container_title | The Journal of biological chemistry |
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| creator | Dutertre, Sébastien Croker, Daniel Daly, Norelle L. Andersson, Åsa Muttenthaler, Markus Lumsden, Natalie G. Craik, David J. Alewood, Paul F. Guillon, Gilles Lewis, Richard J. |
| description | We report the discovery of conopressin-T, a novel bioactive peptide isolated from Conus tulipa venom. Conopressin-T belongs to the vasopressin-like peptide family and displays high sequence homology to the mammalian hormone oxytocin (OT) and to vasotocin, the endogenous vasopressin analogue found in teleost fish, the cone snail's prey. Conopressin-T was found to act as a selective antagonist at the human V1a receptor. All peptides in this family contain two conserved amino acids within the exocyclic tripeptide (Pro7 and Gly9), which are replaced with Leu7 and Val9 in conopressin-T. Whereas conopressin-T binds only to OT and V1a receptors, an L7P analogue had increased affinity for the V1a receptor and weak V2 receptor binding. Surprisingly, replacing Gly9 with Val9 in OT and vasopressin revealed that this position can function as an agonist/antagonist switch at the V1a receptor. NMR structures of both conopressin-T and L7P analogue revealed a marked difference in the orientation of the exocyclic tripeptide that may serve as templates for the design of novel ligands with enhanced affinity for the V1a receptor. |
| doi_str_mv | 10.1074/jbc.M706477200 |
| format | Article |
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Conopressin-T belongs to the vasopressin-like peptide family and displays high sequence homology to the mammalian hormone oxytocin (OT) and to vasotocin, the endogenous vasopressin analogue found in teleost fish, the cone snail's prey. Conopressin-T was found to act as a selective antagonist at the human V1a receptor. All peptides in this family contain two conserved amino acids within the exocyclic tripeptide (Pro7 and Gly9), which are replaced with Leu7 and Val9 in conopressin-T. Whereas conopressin-T binds only to OT and V1a receptors, an L7P analogue had increased affinity for the V1a receptor and weak V2 receptor binding. Surprisingly, replacing Gly9 with Val9 in OT and vasopressin revealed that this position can function as an agonist/antagonist switch at the V1a receptor. NMR structures of both conopressin-T and L7P analogue revealed a marked difference in the orientation of the exocyclic tripeptide that may serve as templates for the design of novel ligands with enhanced affinity for the V1a receptor.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M706477200</identifier><identifier>PMID: 18174156</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Chemical Sciences ; CHO Cells ; Conus Snail - metabolism ; Conus tulipa ; Cricetinae ; Cricetulus ; Humans ; Inositol Phosphates - chemistry ; Life Sciences ; Marine ; Medicinal Chemistry ; Models, Biological ; Oxytocin - analogs & derivatives ; Oxytocin - chemistry ; Oxytocin - metabolism ; Peptides - chemistry ; Receptors, Oxytocin - chemistry ; Receptors, Vasopressin - chemistry ; Toxicology ; Vasopressins - chemistry ; Vasotocin - chemistry</subject><ispartof>The Journal of biological chemistry, 2008-03, Vol.283 (11), p.7100-7108</ispartof><rights>2008 © 2008 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c499t-7d8bd658fedb342d8cb7fd792326b632ba4c0000d7647c45e048c1989d65883d3</citedby><cites>FETCH-LOGICAL-c499t-7d8bd658fedb342d8cb7fd792326b632ba4c0000d7647c45e048c1989d65883d3</cites><orcidid>0000-0002-2945-1484</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18174156$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02306867$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Dutertre, Sébastien</creatorcontrib><creatorcontrib>Croker, Daniel</creatorcontrib><creatorcontrib>Daly, Norelle L.</creatorcontrib><creatorcontrib>Andersson, Åsa</creatorcontrib><creatorcontrib>Muttenthaler, Markus</creatorcontrib><creatorcontrib>Lumsden, Natalie G.</creatorcontrib><creatorcontrib>Craik, David J.</creatorcontrib><creatorcontrib>Alewood, Paul F.</creatorcontrib><creatorcontrib>Guillon, Gilles</creatorcontrib><creatorcontrib>Lewis, Richard J.</creatorcontrib><title>Conopressin-T from Conus tulipa Reveals an Antagonist Switch in Vasopressin-like Peptides</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We report the discovery of conopressin-T, a novel bioactive peptide isolated from Conus tulipa venom. Conopressin-T belongs to the vasopressin-like peptide family and displays high sequence homology to the mammalian hormone oxytocin (OT) and to vasotocin, the endogenous vasopressin analogue found in teleost fish, the cone snail's prey. Conopressin-T was found to act as a selective antagonist at the human V1a receptor. All peptides in this family contain two conserved amino acids within the exocyclic tripeptide (Pro7 and Gly9), which are replaced with Leu7 and Val9 in conopressin-T. Whereas conopressin-T binds only to OT and V1a receptors, an L7P analogue had increased affinity for the V1a receptor and weak V2 receptor binding. Surprisingly, replacing Gly9 with Val9 in OT and vasopressin revealed that this position can function as an agonist/antagonist switch at the V1a receptor. 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NMR structures of both conopressin-T and L7P analogue revealed a marked difference in the orientation of the exocyclic tripeptide that may serve as templates for the design of novel ligands with enhanced affinity for the V1a receptor.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18174156</pmid><doi>10.1074/jbc.M706477200</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0002-2945-1484</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Chemical Sciences CHO Cells Conus Snail - metabolism Conus tulipa Cricetinae Cricetulus Humans Inositol Phosphates - chemistry Life Sciences Marine Medicinal Chemistry Models, Biological Oxytocin - analogs & derivatives Oxytocin - chemistry Oxytocin - metabolism Peptides - chemistry Receptors, Oxytocin - chemistry Receptors, Vasopressin - chemistry Toxicology Vasopressins - chemistry Vasotocin - chemistry |
| title | Conopressin-T from Conus tulipa Reveals an Antagonist Switch in Vasopressin-like Peptides |
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