総説
ロドプシンの結晶化・構造解析
2001 年 41 巻 3 号 p. 142-146
詳細
2001 年 41 巻 3 号 p. 142-146
Recent structure determination of bovine rhodopsin(Rh), a prototypical G protein-coupled receptor(GPCR), by X-ray crystallography has become possible with some noteworthy findings on the selective separation of protein-lipid complex from the natural membrane source and on the phase behavior in crystallization. The structure model of Rh contains much wealth of information explaining how GPCRs can be constrained in their inactive state, and how a number of conserved residues play their roles in the structural frame of GPCRs. A possible mechanism is also presented for the photoactivation of Rh.
