1f88: Difference between revisions

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[[Image:1f88.jpg|left|200px]]<br /><applet load="1f88" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1f88.jpg|left|200px]]
caption="1f88, resolution 2.8&Aring;" />
 
'''CRYSTAL STRUCTURE OF BOVINE RHODOPSIN'''<br />
{{Structure
|PDB= 1f88 |SIZE=350|CAPTION= <scene name='initialview01'>1f88</scene>, resolution 2.8&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=RET:RETINAL'>RET</scene>
|ACTIVITY=
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF BOVINE RHODOPSIN'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1F88 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=RET:'>RET</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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].  
1F88 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. 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==
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10926528 10926528]
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: Bacteriorhodopsin]]
[[Category: Carotenoid Oxygenase]]
[[Category: Carotenoid Oxygenase]]
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[[Category: visual pigment]]
[[Category: visual pigment]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:57 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:44 2008''

Revision as of 12:05, 20 March 2008

File:1f88.jpg


PDB ID 1f88

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands: , and
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

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