1ol6: Difference between revisions

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[[Category: transferase]]
[[Category: transferase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:18:13 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:57:48 2007''

Revision as of 16:53, 30 October 2007

File:1ol6.gif


1ol6, resolution 3.Å

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STRUCTURE OF UNPHOSPHORYLATED D274N MUTANT OF AURORA-A

OverviewOverview

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 StructureAbout this Structure

1OL6 is a [Single protein] structure of sequence from [Homo sapiens] with ATP as [ligand]. Active as [Transferred entry: 2.7.11.1], with EC number [2.7.1.37]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

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

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