2cpk
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(New page: 200px<br /><applet load="2cpk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cpk, resolution 2.7Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 07:05, 21 November 2007
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CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CYCLIC ADENOSINE MONOPHOSPHATE-DEPENDENT PROTEIN KINASE
Overview
The crystal structure of the catalytic subunit of cyclic adenosine, monophosphate-dependent protein kinase complexed with a 20-amino acid, substrate analog inhibitor has been solved and partially refined at 2.7 A, resolution to an R factor of 0.212. The magnesium adenosine triphosphate, (MgATP) binding site was located by difference Fourier synthesis. The, enzyme structure is bilobal with a deep cleft between the lobes. The cleft, is filled by MgATP and a portion of the inhibitor peptide. The smaller, lobe, consisting mostly of amino-terminal sequence, is associated with, nucleotide binding, and its largely antiparallel beta sheet architecture, constitutes an unusual nucleotide binding motif. The larger lobe is, dominated by helical structure with a single beta sheet at the domain, interface. This lobe is primarily involved in peptide binding and, catalysis. Residues 40 through 280 constitute a conserved catalytic core, that is shared by more than 100 protein kinases. Most of the invariant, amino acids in this conserved catalytic core are clustered at the sites of, nucleotide binding and catalysis.
About this Structure
2CPK is a Protein complex structure of sequences from Mus musculus with PO3 as ligand. This structure superseeds the now removed PDB entry 1CPK. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase., Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, Sowadski JM, Science. 1991 Jul 26;253(5018):407-14. PMID:1862342
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