1ol7: Difference between revisions
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[[Image:1ol7. | [[Image:1ol7.jpg|left|200px]]<br /><applet load="1ol7" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1ol7" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1ol7, resolution 2.75Å" /> | caption="1ol7, resolution 2.75Å" /> | ||
'''STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED ON THR287, THR288'''<br /> | '''STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED ON THR287, THR288'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] | 1OL7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OL7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:49:25 2007'' | ||
Revision as of 18:39, 18 December 2007
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STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED ON THR287, THR288
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 phosphothreonine into a, buried position and locking the active conformation. The recognition, between Aurora-A and TPX2 resembles that between the cAPK catalytic core, and its flanking regions, suggesting this molecular mechanism may be a, recurring theme in kinase regulation.
DiseaseDisease
Known diseases associated with this structure: Colon cancer, susceptibility to OMIM:[603072]
About this StructureAbout this Structure
1OL7 is a Single protein structure of sequence from Homo sapiens with MG and ADP as ligands. Active as Transferred entry: 2.7.11.1, with EC number 2.7.1.37 Known structural/functional Site: . 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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