2r4s

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==Crystal structure of the human beta2 adrenoceptor==
==Crystal structure of the human beta2 adrenoceptor==
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<StructureSection load='2r4s' size='340' side='right' caption='[[2r4s]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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<StructureSection load='2r4s' size='340' side='right'caption='[[2r4s]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[2r4s]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2R4S FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r4r|2r4r]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r4s OCA], [https://pdbe.org/2r4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r4s RCSB], [https://www.ebi.ac.uk/pdbsum/2r4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r4s ProSAT]</span></td></tr>
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<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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r4s ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ADRB2_HUMAN 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.
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[https://www.uniprot.org/uniprot/ADRB2_HUMAN 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/2r4s_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/2r4s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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==See Also==
==See Also==
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*[[Nobel Prizes for 3D Molecular Structure|Nobel Prizes for 3D Molecular Structure]]
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*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
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*[[3D structures of monoclonal antibody|3D structures of monoclonal antibody]]
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*[[G protein-coupled receptor|G protein-coupled receptor]]
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*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Burghammer, M]]
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[[Category: Burghammer M]]
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[[Category: Choi, H J]]
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[[Category: Choi HJ]]
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[[Category: Edwards, P C]]
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[[Category: Edwards PC]]
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[[Category: Fischetti, R F]]
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[[Category: Fischetti RF]]
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[[Category: Kobilka, B K]]
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[[Category: Kobilka BK]]
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[[Category: Kobilka, T S]]
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[[Category: Kobilka TS]]
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[[Category: Rasmussen, S G.F]]
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[[Category: Rasmussen SGF]]
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[[Category: Ratnala, V R]]
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[[Category: Ratnala VR]]
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[[Category: Rosenbaum, D M]]
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[[Category: Rosenbaum DM]]
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[[Category: Sanishvili, R]]
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[[Category: Sanishvili R]]
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[[Category: Schertler, G F]]
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[[Category: Schertler GF]]
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[[Category: Thian, F S]]
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[[Category: Thian FS]]
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[[Category: Weis, W I]]
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[[Category: Weis WI]]
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[[Category: G-protein coupled receptor]]
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[[Category: Glycoprotein]]
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[[Category: Lipoprotein]]
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[[Category: Palmitate]]
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[[Category: Phosphorylation]]
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[[Category: Receptor]]
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[[Category: Signaling protein]]
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[[Category: Transducer]]
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[[Category: Transmembrane helix]]
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Current revision

Crystal structure of the human beta2 adrenoceptor

PDB ID 2r4s

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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