{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yuan S"],"funding":["Science and Technology Commission of Shanghai Municipality","Shanghai Frontiers Science Center for Biomacromolecules and Precision Medicine","Beijing Municipal Education Commission","Ministry of Science and Technology of the People&apos;s Republic of China","National Natural Science Foundation of China","ShanghaiTech University","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["992-1007"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10214531"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(5)"],"pubmed_abstract":["Despite advances in characterizing the structures and functions of G protein-coupled receptors (GPCRs), our understanding of GPCR activation and signaling is still limited by the lack of information on conformational dynamics. It is particularly challenging to study the dynamics of GPCR complexes with their signaling partners because of their transient nature and low stability. Here, by combining cross-linking mass spectrometry (CLMS) with integrative structure modeling, we map the conformational ensemble of an activated GPCR-G protein complex at near-atomic resolution. The integrative structures describe heterogeneous conformations for a high number of potential alternative active states of the GLP-1 receptor-G<sub>s</sub> complex. These structures show marked differences from the previou"],"journal":["ACS central science"],"pubmed_title":["Conformational Dynamics of the Activated GLP-1 Receptor-G&lt;sub&gt;s&lt;/sub&gt; Complex Revealed by Cross-Linking Mass Spectrometry and Integrative Structure Modeling."],"pmcid":["PMC10214531"],"funding_grant_id":["32171439","BJJWZYJH01201910001001","31971362","2018YFA0507004","P41GM109824","R01GM083960","21YF1428900","22193073","21661140001","21961142010","P41 GM109824","2022YFA1302902"],"pubmed_authors":["Sun L","Yuan S","Shui W","Xia L","Pan C","Fan Z","Wang C","Lei X","Sali A","Wu F","Zhang B","Stevens RC"],"additional_accession":[]},"is_claimable":false,"name":"Conformational Dynamics of the Activated GLP-1 Receptor-G&lt;sub&gt;s&lt;/sub&gt; Complex Revealed by Cross-Linking Mass Spectrometry and Integrative Structure Modeling.","description":"Despite advances in characterizing the structures and functions of G protein-coupled receptors (GPCRs), our understanding of GPCR activation and signaling is still limited by the lack of information on conformational dynamics. It is particularly challenging to study the dynamics of GPCR complexes with their signaling partners because of their transient nature and low stability. Here, by combining cross-linking mass spectrometry (CLMS) with integrative structure modeling, we map the conformational ensemble of an activated GPCR-G protein complex at near-atomic resolution. The integrative structures describe heterogeneous conformations for a high number of potential alternative active states of the GLP-1 receptor-G<sub>s</sub> complex. These structures show marked differences from the previou","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2026-05-28T22:50:44.188Z","creation":"2025-04-06T00:52:11.104Z"},"accession":"S-EPMC10214531","cross_references":{"pubmed":["37252352"],"doi":["10.1021/acscentsci.3c00063"]}}