{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Woolley MJ"],"funding":["British Heart Foundation","Medical Research Council","Wellcome Trust"],"pagination":["20130589"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3785825"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(88)"],"pubmed_abstract":["The calcitonin gene-related peptide (CGRP) receptor is a complex of a calcitonin receptor-like receptor (CLR), which is a family B G-protein-coupled receptor (GPCR) and receptor activity modifying protein 1. The role of the second extracellular loop (ECL2) of CLR in binding CGRP and coupling to Gs was investigated using a combination of mutagenesis and modelling. An alanine scan of residues 271-294 of CLR showed that the ability of CGRP to produce cAMP was impaired by point mutations at 13 residues; most of these also impaired the response to adrenomedullin (AM). These data were used to select probable ECL2-modelled conformations that are involved in agonist binding, allowing the identification of the likely contacts between the peptide and receptor. The implications of the most likely str"],"journal":["Journal of the Royal Society, Interface"],"pubmed_title":["The role of ECL2 in CGRP receptor activation: a combined modelling and experimental approach."],"pmcid":["PMC3785825"],"funding_grant_id":["PG/12/59/29795","G1001812","091496"],"pubmed_authors":["Karakullukcu ZG","Poyner DR","Taddese B","Hay DL","Reynolds CA","Barwell J","Smith KJ","Woolley MJ","Conner AC","Watkins HA"],"additional_accession":[]},"is_claimable":false,"name":"The role of ECL2 in CGRP receptor activation: a combined modelling and experimental approach.","description":"The calcitonin gene-related peptide (CGRP) receptor is a complex of a calcitonin receptor-like receptor (CLR), which is a family B G-protein-coupled receptor (GPCR) and receptor activity modifying protein 1. The role of the second extracellular loop (ECL2) of CLR in binding CGRP and coupling to Gs was investigated using a combination of mutagenesis and modelling. An alanine scan of residues 271-294 of CLR showed that the ability of CGRP to produce cAMP was impaired by point mutations at 13 residues; most of these also impaired the response to adrenomedullin (AM). These data were used to select probable ECL2-modelled conformations that are involved in agonist binding, allowing the identification of the likely contacts between the peptide and receptor. The implications of the most likely str","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Nov","modification":"2025-04-18T15:54:15.416Z","creation":"2019-03-26T22:41:11Z"},"accession":"S-EPMC3785825","cross_references":{"pubmed":["24047872"],"doi":["10.1098/rsif.2013.0589"]}}