2r4r
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of the human beta2 adrenoceptor== | |
- | === | + | <StructureSection load='2r4r' size='340' side='right' caption='[[2r4r]], [[Resolution|resolution]] 3.40Å' scene=''> |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[2r4r]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. The April 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Adrenergic Receptors'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_4 10.2210/rcsb_pdb/mom_2008_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R4R FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r4s|2r4s]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB2, ADRB2R, B2AR ([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=2r4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r4r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r4r RCSB], [http://www.ebi.ac.uk/pdbsum/2r4r 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/r4/2r4r_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 == | ||
+ | Structural analysis of G-protein-coupled receptors (GPCRs) for hormones and neurotransmitters has been hindered by their low natural abundance, inherent structural flexibility, and instability in detergent solutions. Here we report a structure of the human beta2 adrenoceptor (beta2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop. Diffraction data were obtained by high-brilliance microcrystallography and the structure determined at 3.4 A/3.7 A resolution. The cytoplasmic ends of the beta2AR transmembrane segments and the connecting loops are well resolved, whereas the extracellular regions of the beta2AR are not seen. The beta2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences. These differences may be responsible for the relatively high basal activity and structural instability of the beta2AR, and contribute to the challenges in obtaining diffraction-quality crystals of non-rhodopsin GPCRs. | ||
- | + | Crystal structure of the human beta2 adrenergic G-protein-coupled receptor.,Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK Nature. 2007 Nov 15;450(7168):383-7. Epub 2007 Oct 21. PMID:17952055<ref>PMID:17952055</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
*[[Adrenergic receptor|Adrenergic receptor]] | *[[Adrenergic receptor|Adrenergic receptor]] | ||
*[[G protein-coupled receptor|G protein-coupled receptor]] | *[[G protein-coupled receptor|G protein-coupled receptor]] | ||
+ | *[[Monoclonal Antibody|Monoclonal Antibody]] | ||
*[[Nobel Prizes for 3D Molecular Structure|Nobel Prizes for 3D Molecular Structure]] | *[[Nobel Prizes for 3D Molecular Structure|Nobel Prizes for 3D Molecular Structure]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Adrenergic Receptors]] | [[Category: Adrenergic Receptors]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] |
Revision as of 19:45, 30 September 2014
Crystal structure of the human beta2 adrenoceptor
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Categories: Adrenergic Receptors | Homo sapiens | Mus musculus | RCSB PDB Molecule of the Month | Burghammer, M. | Choi, H J. | Edwards, P C. | Fischetti, R F. | Kobilka, B K. | Kobilka, T S. | Rasmussen, S G.F. | Ratnala, V R. | Rosenbaum, D M. | Sanishvili, R. | Schertler, G F. | Thian, F S. | Weis, W I. | G-protein coupled receptor | Glycoprotein | Lipoprotein | Palmitate | Phosphorylation | Receptor | Signaling protein | Transducer | Transmembrane helix