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Results 1 - 4 of 4
EC Number
Amino acid exchange
Commentary
Reference
C354A
site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe
C354S
site-directed mutagenesis of beta-tubulin, the mutation dramatically reduces the rate of microtubule shrinking and the frequency of catastrophe
T143G
mutation in tubulin signature motif of beta-tubulin, both GTP-binding affinity and microtubule-dependent GTPase activity are reduced at least 15 fold, mutant cells have a delay in mitosis
T238A
naturally occuring mutation, the buried mutation T238A in alphabeta-tubulin yields microtubules with dramatically reduced shrinking rate and catastrophe frequency, the mutation uncouples the tubulin conformational and GTPase cycles, revealing allosteric control of microtubule dynamics. The mutation causes these effects by suppressing a conformational change that normally occurs in response to GTP hydrolysis in the lattice, without detectably changing the conformation of unpolymerized alphabetab-tubulin. The mutation predominantly affects post-GTPase conformational and dynamic properties of microtubules. The buried T238A mutation in beta-tubulin hyperstablizes microtubules in vivo and in vitro. Mutant-induced changes in polymerization dynamics do not result from defective GTPase activity. The T238A alphabeta-tubulin undergoes spontaneous nucleation more readily than wild-type, even in the presence of a nonhydrolyzable GTP analog, GTPgammaS, phenotype, overview
Results 1 - 4 of 4