ISSN:
0887-3585
Keywords:
eye lens proteins
;
protein association
;
crystal packing
;
surface area
;
homologous proteins
;
point mutations
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
A comparative study of intermolecular interactions in crystals of two homologous low molecular weight proteins, γ-II and γ-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 γ-II as compared with 13% in γ-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 γ-II, which are replaced by Met 103 and His 155 in γ-IIIb. A similar substitution of these residues is observed in different gene products of γ-crystallins from a number of vertebrates. This is consistent with the existence of a genetically controlled mechanism for determining intermolecular association of γ-crystallins in the native medium of the lens.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/prot.340040207
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