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Surface interactions of γ-crystallins in the crystal medium in relation to their association in the eye lens

✍ Scribed by Y. V. Sergeev; Y. N. Chirgadze; S. E. Mylvaganam; H. Driessen; C. Slingsby; Dr. T. L. Blundell

Publisher
John Wiley and Sons
Year
1988
Tongue
English
Weight
718 KB
Volume
4
Category
Article
ISSN
0887-3585

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✦ Synopsis

A comparative study of intermolecular interactions in crystals of two homologous low molecular weight proteins, gamma-II and gamma-IIIb crystallins, from calf eye lens was carried out. Crystal packings for these proteins are very different: intermolecular contact areas compose about 33% of the total accessible surface area of gamma-II as compared with 13% in gamma-III. Two key residues seem to be mainly responsible for the differences in protein association in the crystal medium. These are Ser 103 and Leu 155 in gamma-II, which are replaced by Met 103 and His 155 in gamma-IIb. A similar substitution of these residues is observed in different gene products of gamma-crystallins from a number of vertebrates. This is consistent with the existence of a genetically controlled mechanism for determining intermolecular association of gamma-crystallins in the native medium of the lens.

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