5n2r: Difference between revisions
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<StructureSection load='5n2r' size='340' side='right'caption='[[5n2r]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='5n2r' size='340' side='right'caption='[[5n2r]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5n2r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2R OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5n2r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N2R FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8JN:1-butyl-3-[(~{E})-3-oxidanylprop-1-enyl]-8-[(1~{R},5~{S})-3-tricyclo[3.3.1.0^{3,7}]nonanyl]-7~{H}-purine-2,6-dione'>8JN</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8JN:1-butyl-3-[(~{E})-3-oxidanylprop-1-enyl]-8-[(1~{R},5~{S})-3-tricyclo[3.3.1.0^{3,7}]nonanyl]-7~{H}-purine-2,6-dione'>8JN</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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=5n2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n2r OCA], [https://pdbe.org/5n2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n2r RCSB], [https://www.ebi.ac.uk/pdbsum/5n2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n2r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == 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.[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng | [[Category: Cheng RKY]] | ||
[[Category: Cooke | [[Category: Cooke RM]] | ||
[[Category: Deflorian | [[Category: Deflorian F]] | ||
[[Category: Dore | [[Category: Dore AS]] | ||
[[Category: Errey | [[Category: Errey JC]] | ||
[[Category: Fiez-Vandal | [[Category: Fiez-Vandal C]] | ||
[[Category: Marshall | [[Category: Marshall FH]] | ||
[[Category: Robertson | [[Category: Robertson N]] | ||
[[Category: Segala | [[Category: Segala E]] | ||
Latest revision as of 20:59, 8 November 2023
Crystal structure of stabilized A2A adenosine receptor A2AR-StaR2-bRIL in complex with PSB36 at 2.8A resolutionCrystal structure of stabilized A2A adenosine receptor A2AR-StaR2-bRIL in complex with PSB36 at 2.8A resolution
Structural highlights
FunctionAA2AR_HUMAN Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.C562_ECOLX Electron-transport protein of unknown function. Publication Abstract from PubMedThe adenosine A1 and A2A receptors belong to the purinergic family of G protein-coupled receptors, and regulate diverse functions of the cardiovascular, respiratory, renal, inflammation, and CNS. Xanthines such as caffeine and theophylline are weak, non-selective antagonists of adenosine receptors. Here we report the structure of a thermostabilized human A1 receptor at 3.3 A resolution with PSB36, an A1-selective xanthine-based antagonist. This is compared with structures of the A2A receptor with PSB36 (2.8 A resolution), caffeine (2.1 A), and theophylline (2.0 A) to highlight features of ligand recognition which are common across xanthines. The structures of A1R and A2AR were analyzed to identify the differences that are important selectivity determinants for xanthine ligands, and the role of T2707.35 in A1R (M2707.35 in A2AR) in conferring selectivity was confirmed by mutagenesis. The structural differences confirmed to lead to selectivity can be utilized in the design of new subtype-selective A1R or A2AR antagonists. Structures of Human A1 and A2A Adenosine Receptors with Xanthines Reveal Determinants of Selectivity.,Cheng RKY, Segala E, Robertson N, Deflorian F, Dore AS, Errey JC, Fiez-Vandal C, Marshall FH, Cooke RM Structure. 2017 Aug 1;25(8):1275-1285.e4. doi: 10.1016/j.str.2017.06.012. Epub, 2017 Jul 14. PMID:28712806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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