Sandbox 173

From Proteopedia

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Rhodopsin, a dimeric protein, is a highly characterized G protein-coupled receptor found in the neurons of the retina and in rod photoreceptor cells. It is part of the Class A (Family 1) of G protein-coupled receptors, a superfamily of membrane receptors with seven transmembrane helices^[1]. G protein-coupled receptors mediate responses to visual, olfactory, hormonal, and neurotransmitter signals among others^[2].

spinqualitylabelsall models PDB ID 1u19 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1u19, resolution 2.20Å ()
Ligands:	, , , , , , , ,
Non-Standard Residues:
Related:	1f88, 1hzx, 1l9h
Structural annotation: Resources: CATH : 1U19A00, 1U19B00 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

Contents 1 Structure 1.1 Characteristic G Protein-Coupled Receptor Architecture 2 Function 2.1 Light-Induced Visual Signal Transduction 3 Opsin 4 References

Structure

Characteristic G Protein-Coupled Receptor Architecture

Rhodopsin consists of seven mostly α-helical transmembrane domains (H1-H7)linked sequentially by extracellular and cytoplasmic loops (E1-E3 and C1-C3 respectively), with the extracellular amino-terminal tail and the cytoplasmic carboxyl-terminal tail^[3]. Four of the helices are tilted and three of the helices are approximately perpendicular to the membrane plane^[4].

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

1. ↑ Article 6
2. ↑ Article 1
3. ↑ Article 12
4. ↑ Article 4

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