title: alpha-Crystallin quaternary structure: molecular basis for its chaperone activity.
abstract: alpha-Crystallin, the major protein in all vertebrate lenses, functions as a chaperone. In the present analysis, an 'open' micellar structure composed of alpha A subunits is used to simulate chaperoning of partially heat denatured soluble gamma-crystallin. The interaction is both electrostatic and hydrophobic and satisfies experimental evidence for a 1:1 alpha/gamma molar ratio, a doubling of molecular mass and a minimal increase in the dimensions of the complex [J. Biol. Chem. (1994) 269, 13601-13608; Invest. Opthalmol. Vis. Sci. (1995) 36, 311-21]. These data are also in accord with Farahbaksh et al. [Biochemistry (1995) 34, 509-16]; i.e. the bound gamma-crystallin monomers are not in a central cavity, but are separated by alpha A subunits.
authors.affiliation: UMD, Department of Ophthalmology, New Jersey Medical School, Newark, USA.
authors.forename: K
authors.initials: K
authors.lastname: Singh
authors.forename: B
authors.initials: B
authors.lastname: Groth-Vasselli
authors.forename: T F
authors.initials: TF
authors.lastname: Kumosinski
authors.forename: P N
authors.initials: PN
authors.lastname: Farnsworth
mesh_terms: D000595:Amino Acid Sequence; D003459:Crystallins / Q000737:chemistry*; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D003459:Crystallins; D018832:Molecular Chaperones