View source for 4amj


==Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist carvedilol==
<StructureSection load='4amj' size='340' side='right'caption='[[4amj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4amj]] is a 2 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=4AMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AMJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CV:HEGA-10'>2CV</scene>, <scene name='pdbligand=CVD:(2S)-1-(8H-CARBAZOL-4-YLOXY)-3-[2-(2-METHOXYPHENOXY)ETHYLAMINO]PROPAN-2-OL'>CVD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4amj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4amj OCA], [https://pdbe.org/4amj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4amj RCSB], [https://www.ebi.ac.uk/pdbsum/4amj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4amj ProSAT]</span></td></tr>
</table>
== Function ==
[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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The beta(1)-adrenoceptor (beta(1)AR) is the site of action of beta blockers used in the treatment of cardiac-related illnesses. Two beta blockers, carvedilol and bucindolol, show distinctive activities compared to other beta blockers and have been proposed as treatments tailored to the Arg/Gly389(8.56) polymorphism of the human beta(1)AR. Both carvedilol and bucindolol are classified as biased agonists, because they stimulate G protein-independent signaling, while acting as either inverse or partial agonists of the G protein pathway. We have determined the crystal structures of a thermostabilized avian beta(1)AR mutant bound to bucindolol and to carvedilol at 3.2 and 2.3 A resolution, respectively. In comparison to other beta blockers, bucindolol and carvedilol interact with additional residues, in extracellular loop 2 and transmembrane helix 7, which may promote G protein-independent signaling. The structures also suggest that there may be a structural explanation for the pharmacological differences arising from the Arg/Gly389(8.56) polymorphism.

Crystal Structures of a Stabilized beta(1)-Adrenoceptor Bound to the Biased Agonists Bucindolol and Carvedilol.,Warne T, Edwards PC, Leslie AG, Tate CG Structure. 2012 May 9;20(5):841-9. PMID:22579251<ref>PMID:22579251</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4amj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Meleagris gallopavo]]
[[Category: Edwards PC]]
[[Category: Leslie AG]]
[[Category: Tate CG]]
[[Category: Warne T]]