Basak, A. K. and Kroone, R. C. and Lubsen, N. H. and Naylor, C. E. and Jaenicke, Rainer and Slingsby, C. (1998) The C-terminal domains of gamma S-crystallin pair about a distorted twofold axis. PROTEIN ENGINEERING, 11 (5). pp. 337-344. ISSN 0269-2139
Full text not available from this repository.Abstract
The 2-domain gamma S-crystallin, a highly conserved early evolutionary off-shoot of the gamma-crystallin family, is located in the water-rich region of eye lenses. The expressed C-terminal domain, gamma S-C, has been crystallized and the 2.56 Angstrom X-ray structure determined. There are two domains in the asymmetric unit which pair about a distorted twofold axis. One of the domains has an altered conformation in a highly conserved region of the protein, the tyrosine corner. The distorted gamma S-C dimer of domains is compared with the highly symmetrical, equivalent recombinant dimer of C-terminal domains from gamma B-crystallin. Sequence changes close to the interface, that distinguish gamma S from the other gamma-crystallins, are examined in order to evaluate their role in symmetrical domain pairing.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | X-RAY-ANALYSIS; EYE LENS; BETA-CRYSTALLIN; GENE FAMILY; EVOLUTION; PROTEINS; MEMBER; SUPERFAMILY; RESOLUTION; SEQUENCE; gamma S-crystallin; domain interface; lens proteins; tyrosine corner |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 24 Feb 2023 10:14 |
| Last Modified: | 24 Feb 2023 10:14 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49875 |
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