Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study

被引：21

作者：

Csermely, P ^{[1
]}

Miyata, Y ^{[1
]}

Soti, C ^{[1
]}

Yahara, I ^{[1
]}

机构：

[1] TOKYO METROPOLITAN INST MED SCI,DEPT CELL BIOL,BUNKYO KU,TOKYO 113,JAPAN

来源：

LIFE SCIENCES | 1997年 / 61卷 / 04期

关键词：

molecular chaperones; hsp90; calmodulin; casein; histones; surface plasmon resonance;

D O I：

10.1016/S0024-3205(97)00398-6

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

The 90 kDa heat shock protein (hsp90) is a major cytoplasmic molecular chaperone associating with numerous other proteins including steroid receptors. Here we provide the first numerical analysis of hsp90-target associations using surface plasmon resonance. Binding affinities of histones, the ''native molten globule'', casein and calmodulin to hsp90 decrease in the order of K-d = 70 +/- 24, 220 +/- 70 and 1800 +/- 600 nM, respectively. Analysis of the structure of binding proteins revealed that their binding affinity depends on both hydrophobicity and positive charges making the discriminative features of hsp90 similar to those of other molecular chaperones.

引用

页码：411 / 418

页数：8

共 34 条

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