ANALYSIS OF THE COLCHICINE-BINDING SITE OF BETA-TUBULIN

被引：44

作者：

BURNS, RG

机构：

[1] Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, SW7 2BZ, Prince Consort Road

来源：

FEBS LETTERS | 1992年 / 297卷 / 03期

关键词：

BETA-TUBULIN; COLCHICINE BINDING; SEQUENCE ANALYSIS;

D O I：

10.1016/0014-5793(92)80538-R

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：

Comparison of the beta-tubulin sequences with the equilibrium colchicine K(a) and the K(i) for inhibition by podophyllotoxin suggests that residue beta:316 is directly involved in binding the common trimethoxyphenyl-(or A-) ring. By contrast, the analysis indicates that the local hydrophobicity affects the rate of one of the two conformational changes associated with colchicine binding but does not determine the affinity of the colchicine-binding site.

引用

页码：205 / 208

页数：4

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