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Three‐dimensional model and quaternary structure of the human eye lens protein γS‐crystallin based on β‐ and γ‐crystallin X‐ray coordinates and ultracentrifugation
Author(s) -
Zarina S.,
Zaidi Z.H.,
Driessen H.,
Srinivasan N.,
Slingsby C.,
Jaenicke R.
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560031023
Subject(s) - crystallin , protein quaternary structure , monomer , peptide , lens (geology) , chemistry , linker , residue (chemistry) , crystallography , protein structure , analytical ultracentrifugation , ultracentrifuge , eye lens , biophysics , stereochemistry , biochemistry , biology , protein subunit , organic chemistry , computer science , paleontology , gene , operating system , polymer
A 3‐dimensional model of the human eye lens protein γS‐crystallin has been constructed using comparative modeling approaches encoded in the program COMPOSER on the basis of the 3‐dimensional structure of γ‐crystallin and β‐crystallin. The model is biased toward the monomeric γB‐crystallin, which is more similar in sequence. Bovine γS‐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 γ‐crystallins. Because the linker has 1 extra residue compared with γB and βB2, the conformation of the connecting peptide was constructed by using a fragment from a protein database. γS‐crystallin differs from γB‐crystallin mainly in the interface region between domains. The charged residues are generally paired, although in a different way from both β‐ and γ‐crystallins, and may contribute to the different roles of these proteins in the lens.