5iu7: Difference between revisions
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<StructureSection load='5iu7' size='340' side='right'caption='[[5iu7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5iu7' size='340' side='right'caption='[[5iu7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5iu7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5iu7]] 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=5IU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IU7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6DY:2-(FURAN-2-YL)-N~5~-[2-(4-PHENYLPIPERIDIN-1-YL)ETHYL][1,2,4]TRIAZOLO[1,5-A][1,3,5]TRIAZINE-5,7-DIAMINE'>6DY</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=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6DY:2-(FURAN-2-YL)-N~5~-[2-(4-PHENYLPIPERIDIN-1-YL)ETHYL][1,2,4]TRIAZOLO[1,5-A][1,3,5]TRIAZINE-5,7-DIAMINE'>6DY</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=OLB:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLB</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=5iu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iu7 OCA], [https://pdbe.org/5iu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iu7 RCSB], [https://www.ebi.ac.uk/pdbsum/5iu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iu7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</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 == | ||
| Line 27: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bortolato | [[Category: Bortolato A]] | ||
[[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: Guo | [[Category: Guo D]] | ||
[[Category: Heitman | [[Category: Heitman LH]] | ||
[[Category: Ijzerman | [[Category: Ijzerman AP]] | ||
[[Category: Marshall | [[Category: Marshall FH]] | ||
[[Category: Segala | [[Category: Segala E]] | ||
Latest revision as of 17:09, 30 August 2023
Crystal structure of stabilized A2A adenosine receptor A2AR-StaR2-bRIL in complex with compound 12c at 1.9A resolutionCrystal structure of stabilized A2A adenosine receptor A2AR-StaR2-bRIL in complex with compound 12c at 1.9A 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 association and dissociation kinetics of ligands binding to proteins vary considerably, but the mechanisms behind this variability are poorly understood, limiting their utilization for drug discovery. This is particularly so for G protein-coupled receptors (GPCRs) where high resolution structural information is only beginning to emerge. Engineering the human A2A adenosine receptor has allowed structures to be solved in complex with the reference compound ZM241385 and four related ligands at high resolution. Differences between the structures are limited, with the most pronounced being the interaction of each ligand with a salt bridge on the extracellular side of the receptor. Mutagenesis experiments confirm the role of this salt bridge in controlling the dissociation kinetics of the ligands from the receptor, while molecular dynamics simulations demonstrate the ability of ligands to modulate salt bridge stability. These results shed light on a structural determinant of ligand dissociation kinetics and identify a means by which this property may be optimized. Controlling the Dissociation of Ligands from the Adenosine A2A Receptor through Modulation of Salt Bridge Strength.,Segala E, Guo D, Cheng RK, Bortolato A, Deflorian F, Dore AS, Errey JC, Heitman LH, IJzerman AP, Marshall FH, Cooke RM J Med Chem. 2016 Jul 1. PMID:27312113[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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