1gy3
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(New page: 200px<br /> <applet load="1gy3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gy3, resolution 2.7Å" /> '''PCDK2/CYCLIN A IN CO...)
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Revision as of 16:34, 29 October 2007
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PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE SUBSTRATE
Overview
Eukaryotic protein kinases catalyze the phosphoryl transfer of the, gamma-phosphate of ATP to the serine, threonine, or tyrosine residue of, protein substrates. The catalytic mechanism of phospho-CDK2/cyclin A, (pCDK2/cyclin A) has been probed with structural and kinetic studies using, the trigonal NO(3)(-) ion, which can be viewed as a mimic of the, metaphosphate transition state. The crystal structure of pCDK2/cyclin A in, complex with Mg(2+)ADP, nitrate, and a heptapeptide substrate has been, determined at 2.7 A. The nitrate ion is located between the beta-phosphate, of ADP and the hydroxyl group of the serine residue of the substrate. In, one molecule of the asymmetric unit, the nitrate is close to the, beta-phosphate of ADP (distance from the nitrate nitrogen to the nearest, ... [(full description)]
About this Structure
1GY3 is a [Protein complex] structure of sequences from [Homo sapiens] with MG, NO3, ATP and GOL as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structural studies on phospho-CDK2/cyclin A bound to nitrate, a transition state analogue: implications for the protein kinase mechanism., Cook A, Lowe ED, Chrysina ED, Skamnaki VT, Oikonomakos NG, Johnson LN, Biochemistry. 2002 Jun 11;41(23):7301-11. PMID:12044161
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