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Differential effects of colchicine and its B-ring modified analog MTPT on the assembly-independent GTPase activity of purified β-tubulin isoforms from bovine brain
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49. Banerjee A: Differential effects of colchicine and its B-ring modified analog MTPT on the assembly-independent GTPase activity of purified β-tubulin isoforms from bovine brain. Biochem Biophys Res Commun 1997, 231:698-700. This paper complements the large amount of work on colchicine binding with the observation of isotype-specific differences in tubulin's GTPase activation. The B ring of colchicine appears to dominate the interaction with a tubulin and, thus, may be of particular importance in inducing conformational changes at the intradimer interface. Changes in the B ring have different effects on dimers formed with different β isotypes.
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The active GTP-and ground GDP-liganded states of tubulin are distinguished by the binding of chiral isomers of ethyl-5-amino-2-methyl-1,2-dihydro-3-phenylpyrido [3,4-b] pyrazin-7-yl carbamate
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50. Barbier P, Peyrot V, Leynadier D, Andreu JM: The active GTP-and ground GDP-liganded states of tubulin are distinguished by the binding of chiral isomers of ethyl-5-amino-2-methyl-1,2-dihydro-3-phenylpyrido [3,4-b] pyrazin-7-yl carbamate. Biochemistry 1998, 37:758-768. The nucleotide and colchicine-binding sites of tubulin are on nearly opposite sides of the molecule, yet colchicine binding has a significant effect on the intrinsic GTP hydrolysis rate. This paper presents the first demonstration of the fact that the difference between GTP and GDP can effect the binding of a drug at the colchicine site.
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Barbier, P.1
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Andreu, J.M.4
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