1h27: Difference between revisions

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New page: left|200px<br /> <applet load="1h27" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h27, resolution 2.2Å" /> '''CDK2/CYCLIN A IN COM...
 
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==About this Structure==
==About this Structure==
1H27 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=1H27 OCA]].  
1H27 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H27 OCA]].  


==Reference==
==Reference==
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[[Category: serine/threonine-protein kinase]]
[[Category: serine/threonine-protein kinase]]


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Revision as of 13:19, 30 October 2007

File:1h27.gif


1h27, resolution 2.2Å

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CDK2/CYCLIN A IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM P27

OverviewOverview

Progression through S phase of the eukaryotic cell cycle is regulated by, the action of the cyclin dependent protein kinase 2 (CDK2) in association, with cyclin A. CDK2/cyclin A phosphorylates numerous substrates. Substrate, specificity often employs a dual recognition strategy in which the, sequence flanking the phospho-acceptor site (Ser.Pro.X.Arg/Lys) is, recognized by CDK2, while the cyclin A component of the complex contains a, hydrophobic site that binds Arg/Lys.X.Leu ("RXL" or "KXL") substrate, recruitment motifs. To determine additional sequence specificity motifs, around the RXL sequence, we have performed X-ray crystallographic studies, at 2.3 A resolution and isothermal calorimetry measurements on complexes, of phospho-CDK2/cyclin A with a recruitment peptide derived from E2F1 ... [(full description)]

About this StructureAbout this Structure

1H27 is a [Protein complex] structure of sequences from [Homo sapiens]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Specificity determinants of recruitment peptides bound to phospho-CDK2/cyclin A., Lowe ED, Tews I, Cheng KY, Brown NR, Gul S, Noble ME, Gamblin SJ, Johnson LN, Biochemistry. 2002 Dec 31;41(52):15625-34. PMID:12501191

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OCA