Evolution of protein structures and functions

被引:126
作者
Kinch, LN
Grishin, NV
机构
[1] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA
[2] Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA
关键词
D O I
10.1016/S0959-440X(02)00338-X
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
Within the ever-expanding repertoire of known protein sequences and structures, many examples of evolving three-dimensional structures are emerging that illustrate the plasticity and robustness of protein folds. The mechanisms by which protein folds change often include the fusion of duplicated domains, followed by divergence through mutation. Such changes reflect both the stability of protein folds and the requirements of protein function.
引用
收藏
页码:400 / 408
页数:9
相关论文
共 47 条
  • [1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA
    ABRAHAMS, JP
    LESLIE, AGW
    LUTTER, R
    WALKER, JE
    [J]. NATURE, 1994, 370 (6491) : 621 - 628
  • [2] The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    Banner, DW
    DArcy, A
    Chene, C
    Winkler, FK
    Guha, A
    Konigsberg, WH
    Nemerson, Y
    Kirchhofer, D
    [J]. NATURE, 1996, 380 (6569) : 41 - 46
  • [3] Structure and properties of a dimeric N-terminal fragment of human ubiquitin
    Bolton, D
    Evans, PA
    Stott, K
    Broadhurst, RW
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2001, 314 (04) : 773 - 787
  • [4] Crystal structure and mutational analysis the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
    Bourne, Y
    Watson, MH
    Hickey, MJ
    Holmes, W
    Rocque, W
    Reed, SI
    Tainer, JA
    [J]. CELL, 1996, 84 (06) : 863 - 874
  • [5] CRYSTAL-STRUCTURE OF THE CELL CYCLE-REGULATORY PROTEIN SUC1 REVEALS A BETA-HINGE CONFORMATIONAL SWITCH
    BOURNE, Y
    ARVAI, AS
    BERNSTEIN, SL
    WATSON, MH
    REED, SI
    ENDICOTT, JE
    NOBLE, ME
    JOHNSON, LN
    TAINER, JA
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (22) : 10232 - 10236
  • [6] THE BIFUNCTIONAL CYTOCHROME-C REDUCTASE PROCESSING PEPTIDASE COMPLEX FROM PLANT-MITOCHONDRIA
    BRAUN, HP
    SCHMITZ, UK
    [J]. JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1995, 27 (04) : 423 - 436
  • [7] The structure of an engineered domain-swapped ribonuclease dimer and its implications for the evolution of proteins toward oligomerization
    Canals, A
    Pous, J
    Guasch, A
    Benito, A
    Ribó, M
    Vilanova, M
    Coll, M
    [J]. STRUCTURE, 2001, 9 (10) : 967 - 976
  • [8] The N-terminal domain of βB2-crystallin resembles the putative ancestral homodimer
    Clout, NJ
    Basak, A
    Wieligmann, K
    Bateman, OA
    Jaenicke, R
    Slingsby, C
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2000, 304 (03) : 253 - 257
  • [9] The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple βαββ element
    Coles, M
    Diercks, T
    Liermann, J
    Gröger, A
    Rockel, B
    Baumeister, W
    Koretke, KK
    Lupas, A
    Peters, J
    Kessler, H
    [J]. CURRENT BIOLOGY, 1999, 9 (20) : 1158 - 1168
  • [10] Sialidase-like Asp-boxes: Sequence-similar structures within different protein folds
    Copley, RR
    Russell, RB
    Ponting, CP
    [J]. PROTEIN SCIENCE, 2001, 10 (02) : 285 - 292