Structural highlights
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
