1unl

Revision as of 21:06, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1unl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1unl, resolution 2.20Å" /> '''STRUCTURAL MECHANIS...)
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STRUCTURAL MECHANISM FOR THE INHIBITION OF CD5-P25 FROM THE ROSCOVITINE, ALOISINE AND INDIRUBIN.

File:1unl.gif


1unl, resolution 2.20Å

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OverviewOverview

The cyclin-dependent kinases (CDK) CDK1, CDK2, CDK4, and CDK6 are, serine/threonine protein kinases targeted in cancer therapy due to their, role in cell cycle progression. The postmitotic CDK5 is involved in, biological pathways important for neuronal migration and differentiation., CDK5 represents an attractive pharmacological target as its deregulation, is implicated in various neurodegenerative diseases such as Alzheimer's, Parkinson's, and Niemann-Pick type C diseases, ischemia, and amyotrophic, lateral sclerosis. We have generated an improved crystal form of CDK5 in, complex with p25, a segment of the p35 neuronal activator. The crystals, were used to solve the structure of CDK5/p25 with (R)-roscovitine and, aloisine at a resolution of 2.2 and 2.3 A, respectively. The structure of, ... [(full description)]

About this StructureAbout this Structure

1UNL is a [Protein complex] structure of sequences from [Homo sapiens] with RRC as [ligand]. Full crystallographic information is available from [OCA].

ReferenceReference

Mechanism of CDK5/p25 binding by CDK inhibitors., Mapelli M, Massimiliano L, Crovace C, Seeliger MA, Tsai LH, Meijer L, Musacchio A, J Med Chem. 2005 Feb 10;48(3):671-9. PMID:15689152

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