1ol7: Difference between revisions

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[[Image:1ol7.jpg|left|200px]]
[[Image:1ol7.jpg|left|200px]]


{{Structure
<!--
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The line below this paragraph, containing "STRUCTURE_1ol7", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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|DOMAIN=
{{STRUCTURE_1ol7| PDB=1ol7  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ol7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ol7 OCA], [http://www.ebi.ac.uk/pdbsum/1ol7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ol7 RCSB]</span>
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'''STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED ON THR287, THR288'''
'''STRUCTURE OF HUMAN AURORA-A 122-403 PHOSPHORYLATED ON THR287, THR288'''
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[[Category: Bayliss, R.]]
[[Category: Bayliss, R.]]
[[Category: Conti, E.]]
[[Category: Conti, E.]]
[[Category: atp-binding]]
[[Category: Atp-binding]]
[[Category: cell cycle]]
[[Category: Cell cycle]]
[[Category: phosphorylation]]
[[Category: Phosphorylation]]
[[Category: serine/threonine-protein kinase]]
[[Category: Serine/threonine-protein kinase]]
[[Category: transferase]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:59:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:04 2008''

Revision as of 03:59, 3 May 2008

File:1ol7.jpg

Template:STRUCTURE 1ol7

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.

About this StructureAbout this Structure

1OL7 is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Sat May 3 03:59:43 2008

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