1f88: Difference between revisions

Revision as of 17:15, 26 June 2008

Ligands:

, , , ,

Structural annotation:
Resources:	CATH : 1F88A00, 1F88B00 InterPro : Ipr000276, Ipr019477, Ipr017452, Ipr001760, Ipr000732 Pfam : PF00001, PF10413 SCOP : d1f88a_, d1f88b_ UniProt : P02699

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF BOVINE RHODOPSIN

Template:ABSTRACT 10926528

About this StructureAbout this Structure

1F88 is a Single protein structure. The following pages contain interesting information on the relation of 1F88 with [Bacteriorhodopsin], [G Proteins] and [Carotenoid Oxygenase]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 17:15:33 2008

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OCA

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-[[Image:1f88.jpg|left|200px]]
+[[Image:1f88.png|left|200px]]
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-==Overview==
+{{ABSTRACT_10926528}}
-Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural features, including a bundle of seven transmembrane alpha helices connected by six loops of varying lengths. We determined the structure of rhodopsin from diffraction data extending to 2.8 angstroms resolution. The highly organized structure in the extracellular region, including a conserved disulfide bridge, forms a basis for the arrangement of the seven-helix transmembrane motif. The ground-state chromophore, 11-cis-retinal, holds the transmembrane region of the protein in the inactive conformation. Interactions of the chromophore with a cluster of key residues determine the wavelength of the maximum absorption. Changes in these interactions among rhodopsins facilitate color discrimination. Identification of a set of residues that mediate interactions between the transmembrane helices and the cytoplasmic surface, where G-protein activation occurs, also suggests a possible structural change upon photoactivation.
 ==About this Structure==
 F88 is a [[Single protein]] structure. The following pages contain interesting information on the relation of 1F88 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb27_1.html Bacteriorhodopsin]], [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb58_1.html G Proteins]] and [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb66_1.html Carotenoid Oxygenase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F88 OCA].
-==Reference==
-Crystal structure of rhodopsin: A G protein-coupled receptor., Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M, Science. 2000 Aug 4;289(5480):739-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10926528 10926528]
 [[Category: Bacteriorhodopsin]]
 [[Category: Carotenoid Oxygenase]]
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 [[Category: Retinal protein]]
 [[Category: Visual pigment]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:01:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:15:33 2008''

1f88: Difference between revisions

Revision as of 17:15, 26 June 2008

About this StructureAbout this Structure

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