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• W2119736421 abstract "γ-Crystallins are a family of low molecular weight proteins found in high concentration in the densely packed regions of high refractive index in vertebrate lenses. Certain members have the characteristic property of a high critical temperature ( t c ) for phase separation. We report the three-dimensional structure determination of such a protein, bovine lens γIVa-crystallin, which has been refined to give an X-ray R -factor of 0.143. Its high t c contrasts with the low t c γII-crystallin, whose structure we have already published. The root mean square difference between the α-carbon atoms of these two proteins is 0.70 Å and γIVa has an internal symmetry even higher than that of γII. The presence of a protein that exhibits the phenomenon of phase separation at body temperature renders the lens very susceptible to a transformation from transparent to an opaque state due to irregularities in the refractive index. Protein interactions of γIVa-crystallin have implications for the mechanism of cataract formation. Modes of self-association behaviour of γIVa-crystallin have been inferred from an analysis of the lattice interactions in the crystalline state, where the protein packing density is similar to that of the intact lens. It appears that the point mutation at position 103 from a serine residue in γII to a valine in γIVa gives rise to a lattice contact formed by two four-stranded β-sheets in γIVa. A group-specific mutation at position 118 from leucine to phenylalanine induces subtle differences in core packing, leading to a reorganization around residue 103. However, the final phase separation determinant may be a complex combination of many side-chain functions." @default.
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• W2119736421 date "1989-05-01" @default.
• W2119736421 modified "2023-10-16" @default.
• W2119736421 title "Packing interactions in the eye-lens" @default.
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• W2119736421 doi "https://doi.org/10.1016/0022-2836(89)90452-x" @default.
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