1f88: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1f88 |SIZE=350|CAPTION= <scene name='initialview01'>1f88</scene>, resolution 2.8Å | |PDB= 1f88 |SIZE=350|CAPTION= <scene name='initialview01'>1f88</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f88 OCA], [http://www.ebi.ac.uk/pdbsum/1f88 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f88 RCSB]</span> | |||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Palczewski, K.]] | [[Category: Palczewski, K.]] | ||
[[Category: Stenkamp, R E.]] | [[Category: Stenkamp, R E.]] | ||
[[Category: g protein-coupled receptor]] | [[Category: g protein-coupled receptor]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| Line 37: | Line 37: | ||
[[Category: visual pigment]] | [[Category: visual pigment]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:17:54 2008'' | ||
Revision as of 20:17, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF BOVINE RHODOPSIN
OverviewOverview
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 StructureAbout this Structure
1F88 is a Single protein structure of sequence from [1]. 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.
ReferenceReference
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:10926528
Page seeded by OCA on Sun Mar 30 20:17:54 2008