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1h4l

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[[Image:1h4l.gif|left|200px]]
[[Image:1h4l.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1h4l| PDB=1h4l | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4l OCA], [http://www.ebi.ac.uk/pdbsum/1h4l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h4l RCSB]</span>
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'''STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX'''
'''STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX'''
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[[Category: Tarricone, C.]]
[[Category: Tarricone, C.]]
[[Category: Tsai, L H.]]
[[Category: Tsai, L H.]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: cdk5]]
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[[Category: Cdk5]]
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[[Category: cell cycle]]
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[[Category: Cell cycle]]
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[[Category: cell division]]
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[[Category: Cell division]]
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[[Category: cyclin-dependent kinase]]
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[[Category: Cyclin-dependent kinase]]
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[[Category: cyclin]]
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[[Category: Cyclin]]
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[[Category: p25]]
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[[Category: P25]]
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[[Category: p35]]
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[[Category: P35]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:25:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:57:35 2008''
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Revision as of 15:25, 2 May 2008

Image:1h4l.gif


PDB ID 1h4l

Drag the structure with the mouse to rotate
1h4l, resolution 2.65Å ()
Related: 1lfr
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX


Overview

CDK5 plays an indispensable role in the central nervous system, and its deregulation is involved in neurodegeneration. We report the crystal structure of a complex between CDK5 and p25, a fragment of the p35 activator. Despite its partial structural similarity with the cyclins, p25 displays an unprecedented mechanism for the regulation of a cyclin-dependent kinase. p25 tethers the unphosphorylated T loop of CDK5 in the active conformation. Residue Ser159, equivalent to Thr160 on CDK2, contributes to the specificity of the CDK5-p35 interaction. Its substitution with threonine prevents p35 binding, while the presence of alanine affects neither binding nor kinase activity. Finally, we provide evidence that the CDK5-p25 complex employs a distinct mechanism from the phospho-CDK2-cyclin A complex to establish substrate specificity.

About this Structure

1H4L is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure and regulation of the CDK5-p25(nck5a) complex., Tarricone C, Dhavan R, Peng J, Areces LB, Tsai LH, Musacchio A, Mol Cell. 2001 Sep;8(3):657-69. PMID:11583627 Page seeded by OCA on Fri May 2 18:25:26 2008

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