The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis
Author(s) -
A.K. Basak,
R. C. Kroone,
Nicolette H. Lubsen,
C.E. Naylor,
Rainer Jaenicke,
C. Slingsby
Publication year - 1998
Publication title -
protein engineering design and selection
Language(s) - English
Resource type - Journals
eISSN - 1741-0134
pISSN - 1741-0126
DOI - 10.1093/protein/11.5.337
Subject(s) - dimer , crystallography , crystallin , terminal (telecommunication) , domain (mathematical analysis) , sequence (biology) , biophysics , chemistry , physics , biology , nuclear magnetic resonance , biochemistry , computer science , mathematics , mathematical analysis , telecommunications
The 2-domain gammaS-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, gammaS-C, has been crystallized and the 2.56 A 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 gammaS-C dimer of domains is compared with the highly symmetrical, equivalent recombinant dimer of C-terminal domains from gammaB-crystallin. Sequence changes close to the interface, that distinguish gammaS from the other gamma-crystallins, are examined in order to evaluate their role in symmetrical domain pairing.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom