The C-terminal domains of γS-crystallin pair about a distorted twofold axis

被引:13
作者
Basak, AK
Kroone, RC
Lubsen, NH
Naylor, CE
Jaenicke, R
Slingsby, C
机构
[1] Univ London Birkbeck Coll, Dept Crystallog, Mol Biol Lab, London WC1E 7HX, England
[2] Catholic Univ Nijmegen, Dept Biol Mol, NL-6525 ED Nijmegen, Netherlands
[3] Univ Regensburg, Inst Biophys & Phys Biochem, D-93040 Regensburg, Germany
来源
PROTEIN ENGINEERING | 1998年 / 11卷 / 05期
关键词
gamma S-crystallin; domain interface; lens proteins; tyrosine corner;
D O I
10.1093/protein/11.5.337
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:337 / 344
页数:8
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