6lml: Difference between revisions
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The | ==Cryo-EM structure of the human glucagon receptor in complex with Gi1== | ||
<StructureSection load='6lml' size='340' side='right'caption='[[6lml]], [[Resolution|resolution]] 3.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6lml]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LML 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]] 3.9Å</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=6lml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lml OCA], [https://pdbe.org/6lml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lml RCSB], [https://www.ebi.ac.uk/pdbsum/6lml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lml ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Class B G protein-coupled receptors, an important class of therapeutic targets, signal mainly through the Gs class of heterotrimeric G proteins, although they do display some promiscuity in G protein binding. Using cryo-electron microscopy, we determined the structures of the human glucagon receptor (GCGR) bound to glucagon and distinct classes of heterotrimeric G proteins, Gs or Gi1 These two structures adopt a similar open binding cavity to accommodate Gs and Gi1 The Gs binding selectivity of GCGR is explained by a larger interaction interface, but there are specific interactions that affect Gi more than Gs binding. Conformational differences in the receptor intracellular loops were found to be key selectivity determinants. These distinctions in transducer engagement were supported by mutagenesis and functional studies. | |||
Structural basis of Gs and Gi recognition by the human glucagon receptor.,Qiao A, Han S, Li X, Li Z, Zhao P, Dai A, Chang R, Tai L, Tan Q, Chu X, Ma L, Thorsen TS, Reedtz-Runge S, Yang D, Wang MW, Sexton PM, Wootten D, Sun F, Zhao Q, Wu B Science. 2020 Mar 20;367(6484):1346-1352. doi: 10.1126/science.aaz5346. PMID:32193322<ref>PMID:32193322</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6lml" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]] | |||
*[[Glucagon receptor|Glucagon receptor]] | |||
*[[Transducin 3D structures|Transducin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Han S]] | |||
[[Category: Li X]] | |||
[[Category: Qiao A]] | |||
[[Category: Sun F]] | |||
[[Category: Wu B]] | |||
[[Category: Zhao Q]] | |||
Latest revision as of 11:07, 17 October 2024
Cryo-EM structure of the human glucagon receptor in complex with Gi1Cryo-EM structure of the human glucagon receptor in complex with Gi1
Structural highlights
Publication Abstract from PubMedClass B G protein-coupled receptors, an important class of therapeutic targets, signal mainly through the Gs class of heterotrimeric G proteins, although they do display some promiscuity in G protein binding. Using cryo-electron microscopy, we determined the structures of the human glucagon receptor (GCGR) bound to glucagon and distinct classes of heterotrimeric G proteins, Gs or Gi1 These two structures adopt a similar open binding cavity to accommodate Gs and Gi1 The Gs binding selectivity of GCGR is explained by a larger interaction interface, but there are specific interactions that affect Gi more than Gs binding. Conformational differences in the receptor intracellular loops were found to be key selectivity determinants. These distinctions in transducer engagement were supported by mutagenesis and functional studies. Structural basis of Gs and Gi recognition by the human glucagon receptor.,Qiao A, Han S, Li X, Li Z, Zhao P, Dai A, Chang R, Tai L, Tan Q, Chu X, Ma L, Thorsen TS, Reedtz-Runge S, Yang D, Wang MW, Sexton PM, Wootten D, Sun F, Zhao Q, Wu B Science. 2020 Mar 20;367(6484):1346-1352. doi: 10.1126/science.aaz5346. PMID:32193322[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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