View source for 6kr8


==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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</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]]