Crystallographic structure of tubulin: implications for dynamics and drug binding.
The structure of tubulin, recently solved by electron crystallography, has given a first look at the molecular basis for some of the properties of tubulin and microtubules that have been observed over the last decades. We discuss how the structure relates to some of these properties, and how inferences about drug binding sites can explain some of the effects of the drugs on tubulin. Microtubules can form a highly dynamic system that requires careful tuning of the stability and properties of tubulin and its interactions with its many ligands. Understanding these interactions can provide fundamental information on the regulation of the microtubule system.
Downing
K H
KH
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. khdowning@lbl.gov
Nogales
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D001665:Binding Sites; D003078:Colchicine / Q000378:metabolism; D003461:Crystallography; D020558:GTP Phosphohydrolases / Q000502:physiology; D020690:GTPase-Activating Proteins / Q000378:metabolism; D021621:Imaging, Three-Dimensional; D008024:Ligands; D008854:Microscopy, Electron; D008870:Microtubules / Q000378:metabolism; D008958:Models, Molecular; D009711:Nucleotides / Q000378:metabolism; D017239:Paclitaxel / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D014404:Tubulin / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D014747:Vinblastine / Q000378:metabolism
D020690:GTPase-Activating Proteins; D008024:Ligands; D009711:Nucleotides; D014404:Tubulin; D014747:Vinblastine; D020558:GTP Phosphohydrolases; D017239:Paclitaxel; D003078:Colchicine