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
收藏
页码:597 / 627
页数:31
相关论文
共 103 条
[21]   THE PACKING OF ALPHA-HELICES - SIMPLE COILED-COILS [J].
CRICK, FHC .
ACTA CRYSTALLOGRAPHICA, 1953, 6 (8-9) :689-697
[22]   3-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS-STEAROTHERMOPHILUS PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEX [J].
DARDEL, F ;
DAVIS, AL ;
LAUE, ED ;
PERHAM, RN .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 229 (04) :1037-1048
[23]   FAVORED STRUCTURAL MOTIFS IN GLOBULAR-PROTEINS [J].
EFIMOV, AV .
STRUCTURE, 1994, 2 (11) :999-1002
[24]   SUPER-SECONDARY STRUCTURES INVOLVING TRIPLE-STRAND BETA-SHEETS [J].
EFIMOV, AV .
FEBS LETTERS, 1993, 334 (03) :253-256
[25]   Structure of Bordetella pertussis virulence factor P.69 pertactin [J].
Emsley, P ;
Charles, IG ;
Fairweather, NF ;
Isaacs, NW .
NATURE, 1996, 381 (6577) :90-92
[26]   WHY DO GLOBULAR-PROTEINS FIT THE LIMITED SET OF FOLDING PATTERNS [J].
FINKELSTEIN, AV ;
PTITSYN, OB .
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 1987, 50 (03) :171-190
[27]   CRYSTAL-STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-1-BETA AT 2.0-A RESOLUTION [J].
FINZEL, BC ;
CLANCY, LL ;
HOLLAND, DR ;
MUCHMORE, SW ;
WATENPAUGH, KD ;
EINSPAHR, HM .
JOURNAL OF MOLECULAR BIOLOGY, 1989, 209 (04) :779-791
[28]   REFINED STRUCTURE OF ALPHA-LYTIC PROTEASE AT 1.7-A RESOLUTION - ANALYSIS OF HYDROGEN-BONDING AND SOLVENT STRUCTURE [J].
FUJINAGA, M ;
DELBAERE, LTJ ;
BRAYER, GD ;
JAMES, MNG .
JOURNAL OF MOLECULAR BIOLOGY, 1985, 184 (03) :479-502
[29]   REFINED CRYSTAL-STRUCTURE OF THE SERYL-TRANSFER RNA-SYNTHETASE FROM THERMUS-THERMOPHILUS AT 2-CENTER-DOT-5-ANGSTROM RESOLUTION [J].
FUJINAGA, M ;
BERTHETCOLOMINAS, C ;
YAREMCHUK, AD ;
TUKALO, MA ;
CUSACK, S .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 234 (01) :222-233
[30]   STRUCTURE OF CONCANAVALIN-A AT 2.4-A RESOLUTION [J].
HARDMAN, KD ;
AINSWORTH, CF .
BIOCHEMISTRY, 1972, 11 (26) :4910-4919