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 PubMed
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.
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
- ↑ Basak AK, Kroone RC, Lubsen NH, Naylor CE, Jaenicke R, Slingsby C. The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis. Protein Eng. 1998 May;11(5):337-44. PMID:9681865
