Analysis of the colchicine-binding site of beta-tubulin.
Comparison of the beta-tubulin sequences with the equilibrium colchicine Ka and the Ki 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.
Burns
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Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, UK.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003078:Colchicine / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D014404:Tubulin / Q000378:metabolism*
D014404:Tubulin; D003078:Colchicine