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Differential colchicine‐binding across eukaryotic families: The role of highly conserved Pro268β and Ala248β residues in animal tubulin
Author(s) -
Banerjee Mithu,
Roy Debjani,
Bhattacharyya B.,
Basu Gautam
Publication year - 2007
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/j.febslet.2007.09.047
Subject(s) - tubulin , colchicine , microtubule , biology , binding site , microbiology and biotechnology , plasma protein binding , biochemistry , genetics
Colchicine–tubulin interaction, responsible for the disruption of microtubule formation, has immense pharmacological importance but is poorly understood in terms of its biological significance. The interaction is characterized by a marked higher affinity of colchicine for animal tubulins compared to tubulins from plants, fungi and protists. From an analysis of tubulin sequences and colchicine–tubulin crystal structure, we propose that Pro268β and Ala248β (270β and 250β in the crystal structure 1SA0) in animal tubulin are crucial for the observed differential binding. We also suggest that mediated by the binding of endogenous molecules to the colchicine‐binding site, microtubule assembly in eukaryotes may be modulated in a family specific manner.