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Gene Review

MT1A  -  metallothionein-1A

Bos taurus

Synonyms: MT-1A, MT-IA, MT1E, MTC
 
 
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High impact information on MT-1A

  • The binding thermodynamics of colchicine and allocolchicine are similar to MTC under the conditions examined, suggesting related molecular interactions of the three ligands with the protein binding site [1].
  • In addition, allocolchicine binding is about 6 kJ.mol-1 less exothermic than MTC binding, which could be attributed to the presence in allocolchicine of a substituted phenyl ring instead of the colchicine-MTC tropolone ring [1].
  • The kinetics of displacement of the S-isomer by MTC allowed the dissociation rate constant for the S-isomer to be determined [2].
  • Both detergents cause a reduction in the number of tubulin equilibrium binding sites for the colchicine site probe MTC [3].
  • Micelles of octyl glucoside and deoxycholate bind colchicine and its analogue 2-methoxy-5-(2,3,4-trimethoxyphenyl)-2,4,6-cycloheptatrien-1-one (MTC) [3].
 

Anatomical context of MT-1A

  • Spirals of cod microtubule proteins were only formed in the presence of microtubule associated proteins (MAPs), indicating that the morphological effect of MTC can be modulated by MAPs [4].

References

  1. A thermodynamic study of the interaction of tubulin with colchicine site ligands. Menéndez, M., Laynez, J., Medrano, F.J., Andreu, J.M. J. Biol. Chem. (1989) [Pubmed]
  2. Kinetics of association and dissociation of two enantiomers, NSC 613863 (R)-(+) and NSC 613862 (S)-(-) (CI 980), to tubulin. Barbier, P., Peyrot, V., Dumortier, C., D'Hoore, A., Rener, G.A., Engelborghs, Y. Biochemistry (1996) [Pubmed]
  3. Interaction of tubulin with octyl glucoside and deoxycholate. 2. Protein conformation, binding of colchicine ligands, and microtubule assembly. Andreu, J.M., de la Torre, J., Carrascosa, J.L. Biochemistry (1986) [Pubmed]
  4. Comparative study of the colchicine binding site and the assembly of fish and mammalian microtubule proteins. de Pereda, J.M., Wallin, M., Billger, M., Andreu, J.M. Cell Motil. Cytoskeleton (1995) [Pubmed]
 
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