1ol6
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(New page: 200px<br /> <applet load="1ol6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ol6, resolution 3.Å" /> '''STRUCTURE OF UNPHOSPH...)
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Revision as of 15:35, 29 October 2007
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STRUCTURE OF UNPHOSPHORYLATED D274N MUTANT OF AURORA-A
Overview
Aurora-A is an oncogenic kinase essential for mitotic spindle assembly. It, is activated by phosphorylation and by the microtubule-associated protein, TPX2, which also localizes the kinase to spindle microtubules. We have, uncovered the molecular mechanism of Aurora-A activation by determining, crystal structures of its phosphorylated form both with and without a 43, residue long domain of TPX2 that we identified as fully functional for, kinase activation and protection from dephosphorylation. In the absence of, TPX2, the Aurora-A activation segment is in an inactive conformation, with, the crucial phosphothreonine exposed and accessible for deactivation., Binding of TPX2 triggers no global conformational changes in the kinase, but pulls on the activation segment, swinging the ... [(full description)]
About this Structure
1OL6 is a [Single protein] structure of sequence from [Homo sapiens] with ATP as [ligand]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].
Reference
Structural basis of Aurora-A activation by TPX2 at the mitotic spindle., Bayliss R, Sardon T, Vernos I, Conti E, Mol Cell. 2003 Oct;12(4):851-62. PMID:14580337
Page seeded by OCA on Mon Oct 29 17:39:41 2007
