Sandbox 173
From Proteopedia
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Rhodopsin is a G protein-coupled photoreceptor, with seven membrane-spanning α helices embedded in each disk of the outer segments of rod and cone cells in the vertebrate retina. | Rhodopsin is a G protein-coupled photoreceptor, with seven membrane-spanning α helices embedded in each disk of the outer segments of rod and cone cells in the vertebrate retina. | ||
- | The chromophore 11-''cis''-retinal (light-absorbing pigment) is attached to opsin through a Schiff base linkage to | + | The chromophore 11-''cis''-retinal (light-absorbing pigment) is attached to opsin through a Schiff base linkage to Lysine 296. |
{{STRUCTURE_1u19| PDB=1u19 | SCENE= }} | {{STRUCTURE_1u19| PDB=1u19 | SCENE= }} | ||
==Introduction== | ==Introduction== |
Revision as of 21:32, 18 March 2010
Rhodopsin is a G protein-coupled photoreceptor, with seven membrane-spanning α helices embedded in each disk of the outer segments of rod and cone cells in the vertebrate retina. The chromophore 11-cis-retinal (light-absorbing pigment) is attached to opsin through a Schiff base linkage to Lysine 296.
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1u19, resolution 2.20Å () | |||||||||
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Ligands: | , , , , , , , , | ||||||||
Non-Standard Residues: | |||||||||
Related: | 1f88, 1hzx, 1l9h | ||||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
Contents |
Introduction
Structure
Characteristic G Protein-Coupled Receptor Architecture
About this structure[1].
Function
Light-Induced Visual Signal Transduction
Light absorption and G protein activation
Opsin
References
- Okada T, Sugihara M, Bondar AN, Elstner M, Entel P, Buss V. The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure. J Mol Biol. 2004 Sep 10;342(2):571-83. PMID:15327956 doi:10.1016/j.jmb.2004.07.044
- ↑ Testing out reference section, 2010 etc. Yay it works!
Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |