5f8u: Difference between revisions

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<StructureSection load='5f8u' size='340' side='right'caption='[[5f8u]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
<StructureSection load='5f8u' size='340' side='right'caption='[[5f8u]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5f8u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Melga Melga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F8U FirstGlance]. <br>
<table><tr><td colspan='2'>[[5f8u]] 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=5F8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F8U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P32:4-{[(2S)-3-(TERT-BUTYLAMINO)-2-HYDROXYPROPYL]OXY}-3H-INDOLE-2-CARBONITRILE'>P32</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gpo|4gpo]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P32:4-{[(2S)-3-(TERT-BUTYLAMINO)-2-HYDROXYPROPYL]OXY}-3H-INDOLE-2-CARBONITRILE'>P32</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADRB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9103 MELGA])</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=5f8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8u OCA], [https://pdbe.org/5f8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f8u RCSB], [https://www.ebi.ac.uk/pdbsum/5f8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8u ProSAT]</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=5f8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8u OCA], [http://pdbe.org/5f8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8u RCSB], [http://www.ebi.ac.uk/pdbsum/5f8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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 ==
G protein-coupled receptors (GPCRs) mediate transmembrane signaling. Before ligand binding, GPCRs exist in a basal state. Crystal structures of several GPCRs bound with antagonists or agonists have been solved. However, the crystal structure of the ligand-free basal state of a GPCR, the starting point of GPCR activation and function, had not yet been determined. Here we report the X-ray crystal structure of the ligand-free basal state of a GPCR in a lipid membrane-like environment. Oligomeric turkey beta1-adrenergic receptors display two dimer interfaces. One interface involves the transmembrane domain (TM) 1, TM2, the C-terminal H8 and extracellular loop 1. The other interface engages residues from TM4, TM5, intracellular loop 2 and extracellular loop 2. Structural comparisons show that this ligand-free state is in an inactive conformation. This provides the structural basis of GPCR dimerization and oligomerization.
 
Crystal structure of oligomeric beta1-adrenergic G protein-coupled receptors in ligand-free basal state.,Huang J, Chen S, Zhang JJ, Huang XY Nat Struct Mol Biol. 2013 Apr;20(4):419-25. doi: 10.1038/nsmb.2504. Epub 2013 Feb, 24. PMID:23435379<ref>PMID:23435379</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5f8u" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
*[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Melga]]
[[Category: Meleagris gallopavo]]
[[Category: Leslie, A G.W]]
[[Category: Leslie AGW]]
[[Category: Tate, C G]]
[[Category: Tate CG]]
[[Category: Warne, A]]
[[Category: Warne A]]
[[Category: Beta1-ar]]
[[Category: Cyanopindolol]]
[[Category: Signaling protein]]
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