View source for 5g53


==Structure of the adenosine A2A receptor bound to an engineered G protein==
<StructureSection load='5g53' size='340' side='right'caption='[[5g53]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5g53]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G53 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=NEC:N-ETHYL-5-CARBOXAMIDO+ADENOSINE'>NEC</scene>, <scene name='pdbligand=SOG:2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>SOG</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=5g53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g53 OCA], [https://pdbe.org/5g53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g53 RCSB], [https://www.ebi.ac.uk/pdbsum/5g53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g53 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AA2AR_HUMAN AA2AR_HUMAN] Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
G-protein-coupled receptors (GPCRs) are essential components of the signalling network throughout the body. To understand the molecular mechanism of G-protein-mediated signalling, solved structures of receptors in inactive conformations and in the active conformation coupled to a G protein are necessary. Here we present the structure of the adenosine A(2A) receptor (A(2A)R) bound to an engineered G protein, mini-Gs, at 3.4 A resolution. Mini-Gs binds to A(2A)R through an extensive interface (1,048 A2) that is similar, but not identical, to the interface between Gs and the beta2-adrenergic receptor. The transition of the receptor from an agonist-bound active-intermediate state to an active G-protein-bound state is characterized by a 14 A shift of the cytoplasmic end of transmembrane helix 6 (H6) away from the receptor core, slight changes in the positions of the cytoplasmic ends of H5 and H7 and rotamer changes of the amino acid side chains Arg3.50, Tyr5.58 and Tyr7.53. There are no substantial differences in the extracellular half of the receptor around the ligand binding pocket. The A(2A)R-mini-Gs structure highlights both the diversity and similarity in G-protein coupling to GPCRs and hints at the potential complexity of the molecular basis for G-protein specificity.

Structure of the adenosine A(2A) receptor bound to an engineered G protein.,Carpenter B, Nehme R, Warne T, Leslie AG, Tate CG Nature. 2016 Aug 4;536(7614):104-7. PMID:27462812<ref>PMID:27462812</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5g53" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adenosine A2A receptor 3D structures|Adenosine A2A receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Carpenter B]]
[[Category: Leslie AGW]]
[[Category: Nehme R]]
[[Category: Tate CG]]
[[Category: Warne T]]