CRYSTAL-STRUCTURE OF CALF EYE LENS GAMMA-CRYSTALLIN-IIIB AT 2.5-A RESOLUTION - ITS RELATION TO FUNCTION

被引：27

作者：

CHIRGADZE, Y ^{[1
]}

NEVSKAYA, N ^{[1
]}

VERNOSLOVA, E ^{[1
]}

NIKONOV, S ^{[1
]}

SERGEEV, Y ^{[1
]}

BRAZHNIKOV, E ^{[1
]}

FOMENKOVA, N ^{[1
]}

LUNIN, V ^{[1
]}

URZHUMTSEV, A ^{[1
]}

机构：

[1] ACAD SCI USSR,CTR RES COMP,PUSHCHINO 142292,USSR

来源：

EXPERIMENTAL EYE RESEARCH | 1991年 / 53卷 / 03期

关键词：

EYE LENS PROTEIN; GAMMA-CRYSTALLIN-IIIB; PROTEIN STRUCTURE; PROTEIN SURFACE; PROTEIN ASSOCIATION; CHARGES IN PROTEINS;

D O I：

10.1016/0014-4835(91)90233-5

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

The crystal structure of γ-crystallin IIIb (gamma C) from calf eye lens has been refined at 2·5 Å resolution. The molecule of about 21 kDa consists of two similar domains. Each domain is composed of two motifs with the 'Greek key' topology which form a pair of four-stranded β-sheets with an antiparallel packing. The molecule has three hydrophobic cores: one within each domain and one between them. Six of the eight functionally important cysteines are located within the N-domain, and only two in the C-domain. Several large clusters of charged residues are at the surface of the molecule. Surface residues Val 101, Met 103 and Leu 155 are important for packing of molecules in crystal medium and possibly in the lens. Features of the γ-crystallin IIIb molecule which may be related to its function in the vertebrate eye lens are briefly discussed. An attempt has been made to correlate molecular characteristics with some general properties of the eye lens such as high density and refractive index gradients and strong stability of the lens during an organism's lifetime. © 1991.

引用

页码：295 / 304

页数：10

共 33 条

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