title: Analysis of the colchicine-binding site of beta-tubulin.
abstract: 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.
authors.affiliation: Biophysics Section, Blackett Laboratory, Imperial College of Science, Technology and Medicine, London, UK.
authors.forename: R G
authors.initials: RG
authors.lastname: Burns
mesh_terms: 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*
chemical_list: D014404:Tubulin; D003078:Colchicine