The C-terminal domains of gammaS-crystallin pair about a distorted twofold axis.
Protein Eng
; 11(5): 337-44, 1998 May.
Article
en En
| MEDLINE
| ID: mdl-9681865
ABSTRACT
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.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Cristalinas
Límite:
Animals
Idioma:
En
Revista:
Protein Eng
Asunto de la revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
1998
Tipo del documento:
Article
País de afiliación:
Reino Unido