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1h4l

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(New page: 200px<br /> <applet load="1h4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4l, resolution 2.65&Aring;" /> '''STRUCTURE AND REGUL...)
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<applet load="1h4l" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1h4l, resolution 2.65&Aring;" />
'''STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX'''<br />
'''STRUCTURE AND REGULATION OF THE CDK5-P25(NCK5A) COMPLEX'''<br />
==Overview==
==Overview==
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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.
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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1H4L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H4L OCA].
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1H4L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4L OCA].
==Reference==
==Reference==
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[[Category: Peng, J.]]
[[Category: Peng, J.]]
[[Category: Tarricone, C.]]
[[Category: Tarricone, C.]]
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[[Category: Tsai, L.H.]]
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[[Category: Tsai, L H.]]
[[Category: atp-binding]]
[[Category: atp-binding]]
[[Category: cdk5]]
[[Category: cdk5]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:12:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:22 2008''

Revision as of 10:57, 21 February 2008

Image:1h4l.gif

1h4l, resolution 2.65Å

Drag the structure with the mouse to rotate

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

Contents

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.

Disease

Known diseases associated with this structure: Microcephaly, primary autosomal recessive, 3 OMIM:[608201]

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

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