7s1m: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7s1m is ON HOLD
+==Ex4-D-Ala bound to the glucagon-like peptide-1 receptor/g protein complex (conformer 1)==
+<StructureSection load='7s1m' size='340' side='right'caption='[[7s1m]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7s1m]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S1M FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.41&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7s1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s1m OCA], [https://pdbe.org/7s1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s1m RCSB], [https://www.ebi.ac.uk/pdbsum/7s1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s1m ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Recent advances in G-protein-coupled receptor (GPCR) structural elucidation have strengthened previous hypotheses that multidimensional signal propagation mediated by these receptors depends, in part, on their conformational mobility; however, the relationship between receptor function and static structures is inherently uncertain. Here, we examine the contribution of peptide agonist conformational plasticity to activation of the glucagon-like peptide 1 receptor (GLP-1R), an important clinical target. We use variants of the peptides GLP-1 and exendin-4 (Ex4) to explore the interplay between helical propensity near the agonist N terminus and the ability to bind to and activate the receptor. Cryo-EM analysis of a complex involving an Ex4 analog, the GLP-1R and G(s) heterotrimer revealed two receptor conformers with distinct modes of peptide-receptor engagement. Our functional and structural data, along with molecular dynamics (MD) simulations, suggest that receptor conformational dynamics associated with flexibility of the peptide N-terminal activation domain may be a key determinant of agonist efficacy.
-Authors:
+Structural and functional diversity among agonist-bound states of the GLP-1 receptor.,Cary BP, Deganutti G, Zhao P, Truong TT, Piper SJ, Liu X, Belousoff MJ, Danev R, Sexton PM, Wootten D, Gellman SH Nat Chem Biol. 2022 Mar;18(3):256-263. doi: 10.1038/s41589-021-00945-w. Epub 2021 , Dec 22. PMID:34937906<ref>PMID:34937906</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7s1m" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glucagon-like peptide receptor 3D structures|Glucagon-like peptide receptor 3D structures]]
+*[[Transducin 3D structures|Transducin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Lama glama]]
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Cary BP]]
+[[Category: Gellman SH]]