Rhodopsin: structure, signal transduction and oligomerisation.
Rhodopsin was the first G protein-coupled receptor (GPCR) for which a high-resolution crystal structure was obtained. Several crystal structures have now been solved representing different activation states of the receptor. These structures, together with those from lower resolution techniques (e.g. electron microscopy), shed light on the stepwise process by which energy from an extracellular photon is transduced across the membrane to the intracellular compartment thereby activating signalling mechanisms responsible for very low-level light detection. Controversy remains in several areas including: (i) transmembrane helix movements responsible for the transduction process, (ii) the stoichiometry of coupling to G proteins and their mode of activation, (iii) the role, if any, of receptor oligomerisation and (iv) the suitability of using structures of this GPCR as templates for modelling the structures of other GPCRs, and their mechanisms of activation.
Morris
Michael B
MB
Bosch Institute, School of Medical Sciences, University of Sydney, NSW 2006, Australia. michaelmorris@med.usyd.edu.au
Dastmalchi
Siavoush
S
Church
W Bret
WB
D000595:Amino Acid Sequence; D019281:Dimerization; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012174:Retinitis Pigmentosa / Q000378:metabolism; D012243:Rhodopsin / Q000737:chemistry* / Q000378:metabolism*; D015398:Signal Transduction; D013329:Structure-Activity Relationship
D012243:Rhodopsin