1h24
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CDK2/CYCLIN A IN COMPLEX WITH A 9 RESIDUE RECRUITMENT PEPTIDE FROM E2F
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
1H24 is a [Protein complex] structure of sequences from [Homo sapiens]. 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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