Protein folds in the all-beta and all-alpha classes

被引：84

作者：

Chothia, C ^{[1
]}

Hubbard, T ^{[1
]}

Brenner, S ^{[1
]}

Barns, H ^{[1
]}

Murzin, A ^{[1
]}

机构：

[1] CAMBRIDGE CTR PROT ENGN, CAMBRIDGE CB2 2QH, ENGLAND

来源：

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1997年 / 26卷

关键词：

beta-sandwiches; beta-propellers; beta-helices; beta-barrels; beta-prisms; alpha-helix polyhedra; alpha-helix bundles; alpha-helix layer structures; TRANSFER-RNA-SYNTHETASE; CRYSTAL-STRUCTURE; GLOBULAR-PROTEINS; 3-DIMENSIONAL STRUCTURE; CRYSTALLOGRAPHIC REFINEMENT; GEOMETRICAL PROPERTIES; PLEATED SHEETS; 2.2-ANGSTROM RESOLUTION; MOLECULAR-STRUCTURE; BACILLUS-SUBTILIS;

D O I：

10.1146/annurev.biophys.26.1.597

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Analysis of the structures in the Protein Databank, released in June 1996, shows that the number of different protein folds, i.e. the number of different arrangements of major secondary structures and/or chain topologies, is 327. Of these folds, approximately 25% belong to the all-alpha class, 20% belong to the all-beta class, 30% belong to the alpha/beta class, and 25% belong to the alpha + beta class. We describe the types of folds now known for the all-beta and all-alpha classes, emphasizing those that have been discovered recently. Detailed theories for the physical determinants of the structures of most of these folds now exist, and these are reviewed.

引用

页码：597 / 627

页数：31

共 103 条

[51] STRUCTURAL PRINCIPLES OF ALPHA-BETA-BARREL PROTEINS - THE PACKING OF THE INTERIOR OF THE SHEET [J].