The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis |
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Authors: | Basak, AK Kroone, RC Lubsen, NH Naylor, CE Jaenicke, R Slingsby, C |
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Affiliation: | Department of Crystallography, Birkbeck College, London, UK. |
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Abstract: | The 2-domain gammaS-crystallin, a highly conserved early evolutionaryoff-shoot of the gamma-crystallin family, is located in the water-richregion of eye lenses. The expressed C-terminal domain, gammaS-C, has beencrystallized and the 2.56 A X-ray structure determined. There are twodomains in the asymmetric unit which pair about a distorted twofold axis.One of the domains has an altered conformation in a highly conserved regionof the protein, the tyrosine corner. The distorted gammaS-C dimer ofdomains is compared with the highly symmetrical, equivalent recombinantdimer of C-terminal domains from gammaB- crystallin. Sequence changes closeto the interface, that distinguish gammaS from the other gamma-crystallins,are examined in order to evaluate their role in symmetrical domain pairing. |
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