title: Schiff's base formation in the lens protein gamma-crystallin.
abstract: Uniquely among the soluble lens-specific proteins, gamma-crystallin is capable of binding the strongly chromophoric aldehyde retinal. A role for gamma-crystallin in protecting lens components from toxic aldehydes resulting from membrane oxidation is proposed and a molecular model of the probable interaction site is presented. The sequence of a tetrapeptide at this site is identical to that of the retinal binding site of bacteriorhodopsin.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003459:Crystallins / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D012545:Schiff Bases / Q000096:biosynthesis
chemical_list: D003459:Crystallins; D012545:Schiff Bases