1a7h | pdb_00001a7h
From Proteopedia
GAMMA S CRYSTALLIN C-TERMINAL DOMAIN
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Structural highlights
Function[CRBS_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis.,Basak AK, Kroone RC, Lubsen NH, Naylor CE, Jaenicke R, Slingsby C Protein Eng. 1998 May;11(5):337-44. PMID:9681865[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References | ||||||||||||||||||
This page was last modified 10:46, 15 November 2017.