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4gpo

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Revision as of 14:01, 24 December 2014

Oligomeic Turkey Beta1-Adrenergic G Protein-Coupled Receptor

Structural highlights

4gpo is a 2 chain structure with sequence from Meleagris gallopavo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	ADRB1 (Meleagris gallopavo)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Huang J, Chen S, Zhang JJ, Huang XY. Crystal structure of oligomeric beta1-adrenergic G protein-coupled receptors in ligand-free basal state. Nat Struct Mol Biol. 2013 Apr;20(4):419-25. doi: 10.1038/nsmb.2504. Epub 2013 Feb, 24. PMID:23435379 doi:10.1038/nsmb.2504

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gpo"

@@ Line 6: / Line 6: @@
 <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=4gpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gpo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gpo RCSB], [http://www.ebi.ac.uk/pdbsum/4gpo PDBsum]</span></td></tr>
 </table>
+== 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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4gpo

From Proteopedia

Revision as of 14:01, 24 December 2014

Oligomeic Turkey Beta1-Adrenergic G Protein-Coupled Receptor

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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