2r4s: Difference between revisions
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<StructureSection load='2r4s' size='340' side='right' caption='[[2r4s]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='2r4s' size='340' side='right' caption='[[2r4s]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2r4s]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2r4s]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R4S FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r4r|2r4r]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r4r|2r4r]]</td></tr> | ||
<tr id='gene'><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 | <tr id='gene'><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 HUMAN])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r4s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r4s RCSB], [http://www.ebi.ac.uk/pdbsum/2r4s PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r4s OCA], [http://pdbe.org/2r4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r4s RCSB], [http://www.ebi.ac.uk/pdbsum/2r4s PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2r4s" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Burghammer, M]] | [[Category: Burghammer, M]] | ||
Revision as of 10:15, 11 September 2015
Crystal structure of the human beta2 adrenoceptorCrystal structure of the human beta2 adrenoceptor
Structural highlights
Function[ADRB2_HUMAN] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStructural 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Mus musculus
- 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