3d4s
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==Cholesterol bound form of human beta2 adrenergic receptor.== |
+ | <StructureSection load='3d4s' size='340' side='right' caption='[[3d4s]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3d4s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3D4S FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=TIM:(2S)-1-(TERT-BUTYLAMINO)-3-[(4-MORPHOLIN-4-YL-1,2,5-THIADIAZOL-3-YL)OXY]PROPAN-2-OL'>TIM</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rh1|2rh1]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB2, ADRB2R, B2AR / E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3d4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3d4s RCSB], [http://www.ebi.ac.uk/pdbsum/3d4s PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/3d4s_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The role of cholesterol in eukaryotic membrane protein function has been attributed primarily to an influence on membrane fluidity and curvature. We present the 2.8 A resolution crystal structure of a thermally stabilized human beta(2)-adrenergic receptor bound to cholesterol and the partial inverse agonist timolol. The receptors pack as monomers in an antiparallel association with two distinct cholesterol molecules bound per receptor, but not in the packing interface, thereby indicating a structurally relevant cholesterol-binding site between helices I, II, III, and IV. Thermal stability analysis using isothermal denaturation confirms that a cholesterol analog significantly enhances the stability of the receptor. A consensus motif is defined that predicts cholesterol binding for 44% of human class A receptors, suggesting that specific sterol binding is important to the structure and stability of other G protein-coupled receptors, and that this site may provide a target for therapeutic discovery. | ||
- | + | A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor.,Hanson MA, Cherezov V, Griffith MT, Roth CB, Jaakola VP, Chien EY, Velasquez J, Kuhn P, Stevens RC Structure. 2008 Jun;16(6):897-905. PMID:18547522<ref>PMID:18547522</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Adrenergic receptor|Adrenergic receptor]] | *[[Adrenergic receptor|Adrenergic receptor]] | ||
- | *[[ | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure.]] | [[Category: ATCG3D, Accelerated Technologies Center for Gene to 3D Structure.]] |
Revision as of 08:14, 29 September 2014
Cholesterol bound form of human beta2 adrenergic receptor.
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Categories: Homo sapiens | ATCG3D, Accelerated Technologies Center for Gene to 3D Structure. | Cherezov, V. | Chien, E Y.T. | GPCR, GPCR Network. | Griffith, M T. | Hanson, M A. | Jaakola, V-P. | Kuhn, P. | Roth, C B. | Stevens, R C. | Velasquez, J. | Accelerated technologies center for gene to 3d structure | Adrenergic | Atcg3d | Fusion | G-protein coupled receptor | Glycoprotein | Gpcr | Lipoprotein | Lysozyme | Membrane protein | Palmitate | Phosphoprotein | Protein structure initiative | Psi-2 | Receptor | Structural genomic | Timolol | Transducer | Transmembrane