2cch

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spinqualitylabelsall models 2cch, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE CRYSTAL STRUCTURE OF CDK2 CYCLIN A IN COMPLEX WITH A SUBSTRATE PEPTIDE DERIVED FROM CDC MODIFIED WITH A GAMMA-LINKED ATP ANALOGUE

Overview

Phospho-CDK2/cyclin A, a kinase that is active in cell cycle S phase, contains an RXL substrate recognition site that is over 40 A from the, catalytic site. The role of this recruitment site, which enhances, substrate affinity and catalytic efficiency, has been investigated using, peptides derived from the natural substrates, namely CDC6 and p107, and a, bispeptide inhibitor in which the gamma-phosphate of ATP is covalently, attached by a linker to the CDC6 substrate peptide. X-ray studies with a, 30-residue CDC6 peptide in complex with pCDK2/cyclin A showed binding of a, dodecamer peptide at the recruitment site and a heptapeptide at the, catalytic site, but no density for the linking 11 residues. Kinetic, studies established that the CDC6 peptide had an 18-fold lower Km compared, with ... [(full description)]

About this Structure

2CCH is a [Protein complex] structure of sequences from [Homo sapiens] with SO4, ATP and GOL as [ligands]. Full crystallographic information is available from [OCA].

Reference

The role of the phospho-CDK2/cyclin A recruitment site in substrate recognition., Cheng KY, Noble ME, Skamnaki V, Brown NR, Lowe ED, Kontogiannis L, Shen K, Cole PA, Siligardi G, Johnson LN, J Biol Chem. 2006 Aug 11;281(32):23167-79. Epub 2006 May 17. PMID:16707497

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