Analysis of the colchicine‐binding site of β‐tubulin

FEBS Letters

Burns, Roy G.¹ 

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

关键词: β-Tubulin;    Colchicine binding;    Sequence analysis;   

DOI  :  10.1016/0014-5793(92)80538-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Comparison of the β-tubulin sequences with the equilibrium colchicine K _a and the K _i for inhibition by podophyllotoxin suggests that residue β: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.

【 授权许可】

Unknown