Coevolution of the Relaxin-Like Peptides and Their Receptors
: Currently, four relaxin peptide family receptors are known: LGR7 is the relaxin receptor, although it also interacts specifically with relaxin‐3; LGR8 is the insulin‐like factor 3 (INSL3) receptor; and GPCR135 or the somatostatin‐ and angiotensin‐like peptide receptor (SALPR) and GPCR142 are both...
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Veröffentlicht in: | Annals of the New York Academy of Sciences 2005-05, Vol.1041 (1), p.534-539 |
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creator | WILKINSON, TRACEY N. SPEED, TERENCE P. TREGEAR, GEOFFREY W. BATHGATE, ROSS A.D. |
description | : Currently, four relaxin peptide family receptors are known: LGR7 is the relaxin receptor, although it also interacts specifically with relaxin‐3; LGR8 is the insulin‐like factor 3 (INSL3) receptor; and GPCR135 or the somatostatin‐ and angiotensin‐like peptide receptor (SALPR) and GPCR142 are both specific relaxin‐3 receptors. Because these receptors coevolved together with their relaxin ligands, phylogenetic analysis of these sequences can provide insight into peptide‐receptor interactions and even predict interacting partners for INSL4, INSL5, and INSL6, the receptors for which are unknown. |
doi_str_mv | 10.1196/annals.1282.080 |
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Because these receptors coevolved together with their relaxin ligands, phylogenetic analysis of these sequences can provide insight into peptide‐receptor interactions and even predict interacting partners for INSL4, INSL5, and INSL6, the receptors for which are unknown.</description><subject>Animals</subject><subject>coevolution</subject><subject>Evolution, Molecular</subject><subject>Humans</subject><subject>Insulin - genetics</subject><subject>Insulin - metabolism</subject><subject>Ligands</subject><subject>Peptides</subject><subject>phylogenetic analysis</subject><subject>Phylogeny</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Receptors</subject><subject>Receptors, G-Protein-Coupled</subject><subject>Receptors, Peptide - genetics</subject><subject>Receptors, Peptide - metabolism</subject><subject>relaxin receptors</subject><issn>0077-8923</issn><issn>1749-6632</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1LwzAYh4Mobn6cvUlP4qUz32nAyxg6hTHFTcVTyNq3LK5rZ9P58d-b0aE3PQWS5_fLmycInRDcI0TLC1uWtvA9QhPawwneQV2iuI6lZHQXdTFWKk40ZR104P0rxoHjah91iNBCKqG66HJQwXtVrBtXlVGVR80cogco7Kcr45FbQHQPq8Zl4CNbZtF0Dq4O52nYrGp_hPbycD0cb9dD9Hh9NR3cxKO74e2gP4pTTgiPhcBYSEIBmMgA5yLXmlJuRaaBy0SRGYZUiVRLSihhM6zZzKZZJrKEydxydojO2t5VXb2twTdm6XwKRWFLqNbeSKUZwXoDnv8JEkGYwDxJWEAvWjStK-9ryM2qdktbfxmCzcatad2ajVsT3IbE6bZ8PVtC9stvZQaAt8CHK-Drvz4zfulPBNsMHbcx5xv4_InZehEexpQwz-OhGU-un8JHDs0N-wbv8pQa</recordid><startdate>200505</startdate><enddate>200505</enddate><creator>WILKINSON, TRACEY N.</creator><creator>SPEED, TERENCE P.</creator><creator>TREGEAR, GEOFFREY W.</creator><creator>BATHGATE, ROSS A.D.</creator><general>Blackwell Publishing Ltd</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>7SP</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>200505</creationdate><title>Coevolution of the Relaxin-Like Peptides and Their Receptors</title><author>WILKINSON, TRACEY N. ; SPEED, TERENCE P. ; TREGEAR, GEOFFREY W. ; BATHGATE, ROSS A.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4114-55005612ee35de0f5f99224a5d9e46871b0ec75c9621213b093bacdd5d836fa43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>coevolution</topic><topic>Evolution, Molecular</topic><topic>Humans</topic><topic>Insulin - genetics</topic><topic>Insulin - metabolism</topic><topic>Ligands</topic><topic>Peptides</topic><topic>phylogenetic analysis</topic><topic>Phylogeny</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Receptors</topic><topic>Receptors, G-Protein-Coupled</topic><topic>Receptors, Peptide - genetics</topic><topic>Receptors, Peptide - metabolism</topic><topic>relaxin receptors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>WILKINSON, TRACEY N.</creatorcontrib><creatorcontrib>SPEED, TERENCE P.</creatorcontrib><creatorcontrib>TREGEAR, GEOFFREY W.</creatorcontrib><creatorcontrib>BATHGATE, ROSS A.D.</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>Electronics & Communications Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Annals of the New York Academy of Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>WILKINSON, TRACEY N.</au><au>SPEED, TERENCE P.</au><au>TREGEAR, GEOFFREY W.</au><au>BATHGATE, ROSS A.D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Coevolution of the Relaxin-Like Peptides and Their Receptors</atitle><jtitle>Annals of the New York Academy of Sciences</jtitle><addtitle>Ann N Y Acad Sci</addtitle><date>2005-05</date><risdate>2005</risdate><volume>1041</volume><issue>1</issue><spage>534</spage><epage>539</epage><pages>534-539</pages><issn>0077-8923</issn><eissn>1749-6632</eissn><abstract>: Currently, four relaxin peptide family receptors are known: LGR7 is the relaxin receptor, although it also interacts specifically with relaxin‐3; LGR8 is the insulin‐like factor 3 (INSL3) receptor; and GPCR135 or the somatostatin‐ and angiotensin‐like peptide receptor (SALPR) and GPCR142 are both specific relaxin‐3 receptors. 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subjects | Animals coevolution Evolution, Molecular Humans Insulin - genetics Insulin - metabolism Ligands Peptides phylogenetic analysis Phylogeny Proteins - genetics Proteins - metabolism Receptors Receptors, G-Protein-Coupled Receptors, Peptide - genetics Receptors, Peptide - metabolism relaxin receptors |
title | Coevolution of the Relaxin-Like Peptides and Their Receptors |
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