Involvement of colchicine binding site of tubulin in the polymerisation process.
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.
D000107:Acetylation; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000648:ultrastructure; D003078:Colchicine / Q000378:metabolism*; D006041:Goats; D008239:Lysine; D008870:Microtubules / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D013329:Structure-Activity Relationship; D014404:Tubulin / Q000378:metabolism*
D014404:Tubulin; D008239:Lysine; D003078:Colchicine