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α‐Crystallin quaternary structure: molecular basis for its chaperone activity
Author(s) -
Singh Kamalendra,
Groth-Vasselli Barbara,
Kumosinski Thomas F.,
Farnsworth Patricia N.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00980-n
Subject(s) - protein quaternary structure , quaternary , chaperone (clinical) , chemistry , basis (linear algebra) , computational biology , biophysics , biochemistry , microbiology and biotechnology , biology , paleontology , medicine , mathematics , gene , pathology , protein subunit , geometry
α‐Crystallin, the major protein in all vertebrate lenses, functions as a chaperone. In the present analysis, an ‘open’ micellar structure composed of αA subunits is used to simulate chaperoning of partially heat denatured soluble γ‐crystallin. The interaction is both electrostatic and hydrophobic and satisfies experimental evidence for a 1:1 α/γ 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, 311–321]. These data are also in accord with Farahbaksh et al. [Biochemistry (1995) 34, 509–516]; i.e. the bound γ‐crystallin monomers are not in a central cavity, but are separated by αA subunits.