Retinylidene proteins: Structures and functions from archaea to humans

被引：493

作者：

Spudich, JL ^{[1
]}

Yang, CS ^{[1
]}

Jung, KH ^{[1
]}

Spudich, EN ^{[1
]}

机构：

[1] Univ Texas, Sch Med, Dept Microbiol & Mol Genet, Houston, TX 77030 USA

来源：

ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY | 2000年 / 16卷

关键词：

rhodopsin; retinal; vision; photosensory reception; ion transport;

D O I：

10.1146/annurev.cellbio.16.1.365

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Retinylidene proteins, containing seven membrane-embedded alpha -helice that form an internal pocket in which the chromophore retinal is bound, are ubiquitous in photoreceptor cells in eyes throughout the animal kingdom. They are also present in a diverse range of other organisms and locations, such as archaeal prokaryotes, unicellular eukaryotic microbes, the dermal tissue of frogs, the pineal glands of lizards and birds, the hypothalamus of toads, and the human brain. Their functions include light-driven ion transport and phototaxis signaling in microorganisms, and retinal isomerization and various types of photosignal transduction in higher animals. The aims of this review are to examine this group of photoactive proteins as a whole, to summarize our current understanding of structure/function relationships in the best-studied examples, and to report recent new developments.

引用

页码：365 / +

页数：34

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