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Analysis of the colchicine‐binding site of β‐tubulin
Author(s) -
Burns Roy G.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80538-r
Subject(s) - colchicine , podophyllotoxin , tubulin , binding site , chemistry , biophysics , stereochemistry , residue (chemistry) , biochemistry , microtubule , biology , microbiology and biotechnology , genetics
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.