Protein Science, Vol 3, Issue 10 1840-1846, Copyright © 1994 by Cold Spring Harbor Laboratory Press

ARTICLE

Three-dimensional model and quaternary structure of the human eye lens protein {gamma}S-crystallin based on {beta}- and {gamma}-crystallin X-ray coordinates and ultracentrifugation

S. ZARINA, C. SLINGSBY, R. JAENICKE, Z. H. ZAIDI, H. DRIESSEN and N. SRINIVASAN
H.E.J. Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan

A 3-dimensional model of the human eye lens protein {gamma}S-crystallin has been constructed using comparative modeling approaches encoded in the program COMPOSER on the basis of the 3-dimensional structure of {gamma}-crystallin and {beta}-crystallin. The model is biased toward the monomeric {gamma}B-crystallin, which is more similar in sequence. Bovine {gamma}S-crystallin was shown to be monomeric by analytical ultracentrifugation without any tendency to form assemblies up to concentrations in the millimolar range. The connecting peptide between domains was therefore built assuming an intramolecular association as in the monomeric {gamma}-crystallins. Because the linker has 1 extra residue compared with {gamma}B and {beta}B2, the conformation of the connecting peptide was constructed by using a fragment from a protein database. {gamma}S-crystallin differs from {gamma}B-crystallin mainly in the interface region between domains. The charged residues are generally paired, although in a different way from both {beta}- and {gamma}-crystallins, and may contribute to the different roles of these proteins in the lens.
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