-
The molecular structure and stability of the eye lens: x-ray analysis of gamma-crystallin II.
The three-dimensional structure of the eye lens protein, bovine gamma-crystallin II, has been determined at 2.6 A resolution. The protein has a tow domain beta-structure, folded into four remarkably similar 'Greed key' motifs, and shows the highest internal symmetry of any protein studied by X-ray analysis. Although the symmetrical structure seems very stable, the arrangement of the sulphydryl groups would allow intramolecular cross-linking leading to possible destabilization, and intermolecular cross-linking leading to aggregation, both of which may be important to cataract formation.
PMID: 7464942 [PubMed - indexed for MEDLINE]
-
Cited by 46 PubMed Central articles
-
Mutation analysis of CRYAA, CRYGC, and CRYGD associated with autosomal dominant congenital cataract in Brazilian families.
Santana A, Waiswol M, Arcieri ES, Cabral de Vasconcellos JP, Barbosa de Melo M.
Mol Vis. 2009; 15:793-800. Epub 2009 Apr 17.
[Mol Vis. 2009]
-
Novel mutation in the gamma-S crystallin gene causing autosomal dominant cataract.
Vanita V, Singh JR, Singh D, Varon R, Sperling K.
Mol Vis. 2009; 15:476-81. Epub 2009 Mar 4.
[Mol Vis. 2009]
-
A novel nonsense mutation in CRYGC is associated with autosomal dominant congenital nuclear cataracts and microcornea.
Zhang L, Fu S, Ou Y, Zhao T, Su Y, Liu P.
Mol Vis. 2009; 15:276-82. Epub 2009 Feb 6.
[Mol Vis. 2009]
- » See all...
Structures reported by this article