2vt4

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[[Image:2vt4.jpg|left|200px]]
 
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==TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL==
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The line below this paragraph, containing "STRUCTURE_2vt4", creates the "Structure Box" on the page.
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<StructureSection load='2vt4' size='340' side='right'caption='[[2vt4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vt4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VT4 FirstGlance]. <br>
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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]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P32:4-{[(2S)-3-(TERT-BUTYLAMINO)-2-HYDROXYPROPYL]OXY}-3H-INDOLE-2-CARBONITRILE'>P32</scene>, <scene name='pdbligand=SOG:2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>SOG</scene></td></tr>
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{{STRUCTURE_2vt4| PDB=2vt4 | SCENE= }}
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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=2vt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vt4 OCA], [https://pdbe.org/2vt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2vt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vt4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADRB1_MELGA ADRB1_MELGA] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vt/2vt4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2vt4 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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G-protein-coupled receptors have a major role in transmembrane signalling in most eukaryotes and many are important drug targets. Here we report the 2.7 A resolution crystal structure of a beta(1)-adrenergic receptor in complex with the high-affinity antagonist cyanopindolol. The modified turkey (Meleagris gallopavo) receptor was selected to be in its antagonist conformation and its thermostability improved by earlier limited mutagenesis. The ligand-binding pocket comprises 15 side chains from amino acid residues in 4 transmembrane alpha-helices and extracellular loop 2. This loop defines the entrance of the ligand-binding pocket and is stabilized by two disulphide bonds and a sodium ion. Binding of cyanopindolol to the beta(1)-adrenergic receptor and binding of carazolol to the beta(2)-adrenergic receptor involve similar interactions. A short well-defined helix in cytoplasmic loop 2, not observed in either rhodopsin or the beta(2)-adrenergic receptor, directly interacts by means of a tyrosine with the highly conserved DRY motif at the end of helix 3 that is essential for receptor activation.
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'''TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL'''
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Structure of a beta1-adrenergic G-protein-coupled receptor.,Warne T, Serrano-Vega MJ, Baker JG, Moukhametzianov R, Edwards PC, Henderson R, Leslie AG, Tate CG, Schertler GF Nature. 2008 Jul 24;454(7203):486-91. Epub 2008 Jun 25. PMID:18594507<ref>PMID:18594507</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2vt4" style="background-color:#fffaf0;"></div>
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{{ABSTRACT_18192400}}
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==See Also==
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*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
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==About this Structure==
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== References ==
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2VT4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VT4 OCA].
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Meleagris gallopavo]]
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[[Category: Single protein]]
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[[Category: Baker JG]]
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[[Category: Baker, J G.]]
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[[Category: Edwards PC]]
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[[Category: Edwards, P C.]]
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[[Category: Henderson R]]
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[[Category: Henderson, R.]]
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[[Category: Leslie AGW]]
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[[Category: Leslie, A G.W.]]
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[[Category: Moukhametzianov R]]
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[[Category: Moukhametzianov, R.]]
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[[Category: Schertler GFX]]
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[[Category: Schertler, G F.X.]]
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[[Category: Serrano-Vega MJ]]
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[[Category: Serrano-Vega, M J.]]
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[[Category: Tate CG]]
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[[Category: Tate, C G.]]
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[[Category: Warne A]]
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[[Category: Warne, A.]]
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[[Category: 7tm receptor]]
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[[Category: Antagonist bound form]]
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[[Category: G protein coupled receptor]]
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[[Category: G-protein coupled receptor]]
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[[Category: Glycoprotein]]
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[[Category: Gpcr]]
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[[Category: Integral membrane protein]]
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[[Category: Lipoprotein]]
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[[Category: Membrane]]
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[[Category: Palmitate]]
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[[Category: Phosphoprotein]]
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[[Category: Receptor]]
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[[Category: Seven-helix receptor]]
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[[Category: Thermostabilising point mutation]]
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[[Category: Transducer]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 18:52:22 2008''
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Current revision

TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL

PDB ID 2vt4

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