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| | ==Oligomeic Turkey Beta1-Adrenergic G Protein-Coupled Receptor== | | ==Oligomeic Turkey Beta1-Adrenergic G Protein-Coupled Receptor== |
| - | <StructureSection load='4gpo' size='340' side='right' caption='[[4gpo]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='4gpo' size='340' side='right'caption='[[4gpo]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gpo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Common_turkey Common turkey]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GPO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gpo]] 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=4GPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GPO FirstGlance]. <br> |
| - | </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 Common turkey])</td></tr> | + | </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=4gpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gpo OCA], [https://pdbe.org/4gpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gpo RCSB], [https://www.ebi.ac.uk/pdbsum/4gpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gpo 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=4gpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gpo OCA], [http://pdbe.org/4gpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gpo RCSB], [http://www.ebi.ac.uk/pdbsum/4gpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gpo 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Adrenergic receptor|Adrenergic receptor]] | + | *[[Adrenergic receptor 3D structures|Adrenergic receptor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Common turkey]] | + | [[Category: Large Structures]] |
| - | [[Category: Chen, S]] | + | [[Category: Meleagris gallopavo]] |
| - | [[Category: Huang, J J]] | + | [[Category: Chen S]] |
| - | [[Category: Huang, X Y]] | + | [[Category: Huang JJ]] |
| - | [[Category: Zhang, J J]] | + | [[Category: Huang XY]] |
| - | [[Category: G-protein coupled receptor]] | + | [[Category: Zhang JJ]] |
| - | [[Category: Receptor]]
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| - | [[Category: Seven-transmembrane helix receptor]]
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| Structural highlights
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.
See Also
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
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