NDLI: 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.

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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.

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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.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Srinivasan, N. Slingsby, C. Driessen, H. Zarina, S. Jaenicke, R. Zaidi, Z. H.
Description	Country affiliation: Pakistan Author Affiliation: Zarina S ( H.E.J. Research Institute of Chemistry, University of Karachi, Pakistan.)
Abstract	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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	10
Volume Number	3
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1994-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Crystallins Chemistry Crystallography, X-ray Models, Molecular Amino Acid Sequence Animals Computer Simulation Cysteine Electrochemistry Macromolecular Substances Methionine Molecular Sequence Data Molecular Weight Peptide Fragments Protein Conformation Ultracentrifugation Comparative Study Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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