Protein-biotin interactions

被引：32

作者：

Lindqvist, Y

Schneider, G

机构：

[1] Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77 Stockholm

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1996年 / 6卷 / 06期

关键词：

D O I：

10.1016/S0959-440X(96)80010-8

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：

The three-dimensional structures of several biotin-binding proteins are now known, giving insights into the molecular architecture of the binding sites for biotin. In combination with biochemical and computational approaches, these structural insights provide the basis for our present understanding of biotin-protein interactions which, in some cases, give rise to spectacular binding constants.

引用

收藏

页码：798 / 803

页数：6

相关论文

共 46 条

[1] COOPERATIVE BINDING OF THE ESCHERICHIA-COLI REPRESSOR OF BIOTIN BIOSYNTHESIS TO THE BIOTIN OPERATOR SEQUENCE [J].

ABBOTT, J ;

BECKETT, D .

BIOCHEMISTRY, 1993, 32 (37) :9649-9656

[2] SUBSTRATE-BINDING AND CARBOXYLATION BY DETHIOBIOTIN SYNTHETASE - A KINETIC AND X-RAY STUDY [J].

ALEXEEV, D ;

BAXTER, RL ;

SMEKAL, O ;

SAWYER, L .

STRUCTURE, 1995, 3 (11) :1207-1215

[3] MECHANISTIC IMPLICATIONS AND FAMILY RELATIONSHIPS FROM THE STRUCTURE OF DETHIOBIOTIN SYNTHETASE [J].

ALEXEEV, D ;

BAXTER, RL ;

SAWYER, L .

STRUCTURE, 1994, 2 (11) :1061-1072

[4] Biotin carboxylase comes into the fold [J].

Artymiuk, PJ ;

Poirrette, AR ;

Rice, DW ;

Willett, P .

NATURE STRUCTURAL BIOLOGY, 1996, 3 (02) :128-132

[5]

ARTYMUIK PJ, 1994, NAT STRUCT BIOL, V7, P758

[6] Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing [J].

Athappilly, FK ;

Hendrickson, WA .

STRUCTURE, 1995, 3 (12) :1407-1419

[7] MOLECULAR-ORIGINS OF THE SLOW STREPTAVIDIN-BIOTIN DISSOCIATION KINETICS [J].

CHILKOTI, A ;

STAYTON, PS .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (43) :10622-10628

[8] SITE-DIRECTED MUTAGENESIS STUDIES OF THE HIGH-AFFINITY STREPTAVIDIN-BIOTIN COMPLEX - CONTRIBUTIONS OF TRYPTOPHAN RESIDUE-79, RESIDUE-108, AND RESIDUE-120 [J].

CHILKOTI, A ;

TAN, PH ;

STAYTON, PS .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (05) :1754-1758

[9] The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy [J].

Chilkoti, A ;

Boland, T ;

Ratner, BD ;

Stayton, PS .

BIOPHYSICAL JOURNAL, 1995, 69 (05) :2125-2130

[10] THE ESCHERICHIA-COLI BIO-OPERON - TRANSCRIPTIONAL REPRESSION BY AN ESSENTIAL PROTEIN MODIFICATION ENZYME [J].

CRONAN, JE .

CELL, 1989, 58 (03) :427-429

← 1 2 3 4 5 →