PMID: 6404647Feb 7, 1983Paper

Involvement of colchicine binding site of tubulin in the polymerisation process

FEBS Letters
D DasguptaS Gurnani

Abstract

Role of lysine residues in the colchicine binding site and in the assembly-disassembly process was examined. It was observed that at 4 degrees C (pH 7.5-8, 8 +/- 1) lysine residues and the N-terminal methionine residue of tubulin were all buried within the molecule. Evidence indicates that epsilon-amino groups of lysine residues of tubulin are shared by both the colchicine binding site and the polymerisation process.

References

Jan 1, 1976·Annual Review of Biochemistry·J A Snyder, J R McIntosh
May 21, 1974·Biochemistry·B Bhattacharyya, J Wolff
Apr 22, 1969·Biochimica Et Biophysica Acta·R C Davies, A Neuberger
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS

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Citations

Oct 1, 1985·Biochemical Pharmacology·R Rajagopalan, S Gurnani
Nov 1, 1986·Chemico-biological Interactions·R Rajagopalan, S Gurnani
Oct 14, 1983·Biochemical and Biophysical Research Communications·R Rajagopalan, S Gurnani
Jul 1, 1987·Cell Biochemistry and Function·A MigliettaE Gadoni
Jan 15, 2016·The Journal of Biological Chemistry·Shuchen GuXin-Hua Feng
Oct 14, 2010·Cellular Signalling·Daniel PerdizAnita Baillet

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