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
收藏
页码：205 / 208
页数：4
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