6kr8: Difference between revisions
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New page: '''Unreleased structure''' The entry 6kr8 is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Structure of the beta2 adrenergic receptor in the full agonist bound state== | |||
<StructureSection load='6kr8' size='340' side='right'caption='[[6kr8]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6kr8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KR8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KR8 FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6kr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kr8 OCA], [http://pdbe.org/6kr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kr8 RCSB], [http://www.ebi.ac.uk/pdbsum/6kr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kr8 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
G-protein-coupled receptors (GPCRs) are seven-transmembrane proteins mediating cellular signals in response to extracellular stimuli. Although three-dimensional structures showcase snapshots that can be sampled in the process and nuclear magnetic resonance detects conformational equilibria, the mechanism by which agonist-activated GPCRs interact with various effectors remains elusive. Here, we used paramagnetic nuclear magnetic resonance for leucine amide resonances to visualize the structure of beta2-adrenoreceptor in the full agonist-bound state, without thermostabilizing mutations abolishing its activity. The structure exhibited a unique orientation of the intracellular half of the transmembrane helix 6, forming a cluster of G-protein-interacting residues. Furthermore, analyses of efficacy-dependent chemical shifts of the residues near the pivotal PIF microswitch identified an equilibrium among three conformations, including one responsible for the varied signal level in each ligand-bound state. Together, these results provide a structural basis for the dynamic activation of GPCRs and shed light on GPCR-mediated signal transduction. | |||
Structural equilibrium underlying ligand-dependent activation of beta2-adrenoreceptor.,Imai S, Yokomizo T, Kofuku Y, Shiraishi Y, Ueda T, Shimada I Nat Chem Biol. 2020 Jan 20. pii: 10.1038/s41589-019-0457-5. doi:, 10.1038/s41589-019-0457-5. PMID:31959965<ref>PMID:31959965</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6kr8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Large Structures]] | |||
[[Category: Imai, S]] | |||
[[Category: Shimada, I]] | |||
[[Category: B2ar]] | |||
[[Category: Full agonist]] | |||
[[Category: G-protein coupled receptor]] | |||
[[Category: Membrane protein]] | |||
