MODELING MUTATIONS AND HOMOLOGOUS PROTEINS

被引：124

作者：

SALI, A

机构：

来源：

CURRENT OPINION IN BIOTECHNOLOGY | 1995年 / 6卷 / 04期

关键词：

D O I：

10.1016/0958-1669(95)80074-3

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A protein sequence with at least 40% identity to a known structure can now be modelled automatically, with an accuracy approaching that of a low-resolution X-ray structure or a medium-resolution nuclear magnetic resonance structure. In general, these models have good stereochemistry and an overall structural accuracy that is as high as the similarity between the template and the actual structure being predicted. As a result, the number of sequences that can be modelled is an order of magnitude larger than the number of experimentally determined protein structures. In addition, evaluation techniques are available that can estimate errors in different regions of the model. Thus, the number of applications where homology modelling is proving useful is growing rapidly.

引用

收藏

页码：437 / 451

页数：15

相关论文

共 222 条

[31] THE FREQUENCY OF ION-PAIR SUBSTRUCTURES IN PROTEINS IS QUANTITATIVELY RELATED TO ELECTROSTATIC POTENTIAL - A STATISTICAL-MODEL FOR NONBONDED INTERACTIONS [J].

BRYANT, SH ;

LAWRENCE, CE .

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 1991, 9 (02) :108-119

[32]

BRYANT SH, 1987, INT J PEPT PROT RES, V29, P46

[33] AN EMPIRICAL ENERGY FUNCTION FOR THREADING PROTEIN-SEQUENCE THROUGH THE FOLDING MOTIF [J].

BRYANT, SH ;

LAWRENCE, CE .

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 1993, 16 (01) :92-112

[34] CONVERSION OF THE SUBSTRATE-SPECIFICITY OF MOUSE PROTEINASE GRANZYME-B [J].

CAPUTO, A ;

JAMES, MNG ;

POWERS, JC ;

HUDIG, D ;

BLEACKLEY, RC .

NATURE STRUCTURAL BIOLOGY, 1994, 1 (06) :364-367

[35] COMPARISON OF HOMOLOGY MODELS WITH THE EXPERIMENTAL STRUCTURE OF A NOVEL SERINE-PROTEASE [J].

CARSON, M ;

BUGG, CE ;

DELUCAS, LJ ;

NARAYANA, SVL .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1994, 50 :889-899

[36] EASY ADAPTATION OF PROTEIN-STRUCTURE TO SEQUENCE [J].

CHELVANAYAGAM, G ;

ROY, G ;

ARGOS, P .

PROTEIN ENGINEERING, 1994, 7 (02) :173-184

[37] PROTEIN MODEL STRUCTURE EVALUATION USING THE SOLVATION FREE-ENERGY OF FOLDING [J].

CHICHE, L ;

GREGORET, LM ;

COHEN, FE ;

KOLLMAN, PA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (08) :3240-3243

[38] CONFORMATIONS OF IMMUNOGLOBULIN HYPERVARIABLE REGIONS [J].

CHOTHIA, C ;

LESK, AM ;

TRAMONTANO, A ;

LEVITT, M ;

SMITHGILL, SJ ;

AIR, G ;

SHERIFF, S ;

PADLAN, EA ;

DAVIES, D ;

TULIP, WR ;

COLMAN, PM ;

SPINELLI, S ;

ALZARI, PM ;

POLJAK, RJ .

NATURE, 1989, 342 (6252) :877-883

[39] THE PREDICTED STRUCTURE OF IMMUNOGLOBULIN-D1.3 AND ITS COMPARISON WITH THE CRYSTAL-STRUCTURE [J].

CHOTHIA, C ;

LESK, AM ;

LEVITT, M ;

AMIT, AG ;

MARIUZZA, RA ;

PHILLIPS, SEV ;

POLJAK, RJ .

SCIENCE, 1986, 233 (4765) :755-758

[40] PROTEINS - 1000 FAMILIES FOR THE MOLECULAR BIOLOGIST [J].

CHOTHIA, C .

NATURE, 1992, 357 (6379) :543-544

← 1 2 3 4 5 6 7 8 9 10 →