A structural view of microtubule dynamics.
The essential microtubule property of dynamic instability is based on the binding, hydrolysis and exchange of GTP in each tubulin dimer. The recent high-resolution structures of tubulin and the microtubule have given us the first view at atomic level of properties such as nucleotide exchangeability, the linkage between polymerization and nucleotide hydrolysis. and the origin of microtubule destabilization, as well as the mode of action of antimitotic agents such as taxol.
Nogales
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Department of Molecular and Cell Biology, UC Berkeley, California 94720-3200, USA. enogales@lbl.gov
D000595:Amino Acid Sequence; D000972:Antineoplastic Agents, Phytogenic / Q000494:pharmacology; D003461:Crystallography; D019281:Dimerization; D006160:Guanosine Triphosphate / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry* / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017239:Paclitaxel / Q000494:pharmacology; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D014404:Tubulin / Q000737:chemistry
D000972:Antineoplastic Agents, Phytogenic; D014404:Tubulin; D006160:Guanosine Triphosphate; D017239:Paclitaxel