2cci

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[[Image:2cci.gif|left|200px]]
[[Image:2cci.gif|left|200px]]
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{{Structure
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|PDB= 2cci |SIZE=350|CAPTION= <scene name='initialview01'>2cci</scene>, resolution 2.70&Aring;
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The line below this paragraph, containing "STRUCTURE_2cci", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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|DOMAIN=
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{{STRUCTURE_2cci| PDB=2cci | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cci OCA], [http://www.ebi.ac.uk/pdbsum/2cci PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cci RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF PHOSPHO-CDK2 CYCLIN A IN COMPLEX WITH A PEPTIDE CONTAINING BOTH THE SUBSTRATE AND RECRUITMENT SITES OF CDC6'''
'''CRYSTAL STRUCTURE OF PHOSPHO-CDK2 CYCLIN A IN COMPLEX WITH A PEPTIDE CONTAINING BOTH THE SUBSTRATE AND RECRUITMENT SITES OF CDC6'''
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[[Category: Siligardi, G.]]
[[Category: Siligardi, G.]]
[[Category: Skamnaki, V.]]
[[Category: Skamnaki, V.]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: cell cycle]]
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[[Category: Cell cycle]]
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[[Category: cell division]]
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[[Category: complex]]
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[[Category: Complex]]
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[[Category: cyclin]]
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[[Category: Cyclin]]
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[[Category: dna replication]]
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[[Category: Dna replication]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: mitosis]]
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[[Category: nuclear protein]]
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[[Category: nucleotide-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphorylation]]
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[[Category: protein kinase]]
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[[Category: Protein kinase]]
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[[Category: recruitment]]
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[[Category: Recruitment]]
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[[Category: serine/threonine-protein kinase]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: substrate recognition]]
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[[Category: Substrate recognition]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:47:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:19:35 2008''
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Revision as of 18:47, 3 May 2008

Image:2cci.gif

Template:STRUCTURE 2cci

CRYSTAL STRUCTURE OF PHOSPHO-CDK2 CYCLIN A IN COMPLEX WITH A PEPTIDE CONTAINING BOTH THE SUBSTRATE AND RECRUITMENT SITES OF CDC6


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 heptapeptide substrate and that this effect required the recruitment peptide to be covalently linked to the substrate peptide. X-ray studies with the CDC6 bispeptide showed binding of the dodecamer at the recruitment site and the modified ATP in two alternative conformations at the catalytic site. The CDC6 bispeptide was a potent inhibitor competitive with both ATP and peptide substrate of pCDK2/cyclin A activity against a heptapeptide substrate (Ki = 0.83 nm) but less effective against RXL-containing substrates. We discuss how localization at the recruitment site (KD 0.4 microm) leads to increased catalytic efficiency and the design of a potent inhibitor. The notion of a flexible linker between the sites, which must have more than a minimal number of residues, provides an explanation for recognition and discrimination against different substrates.

About this Structure

2CCI is a Protein complex structure of sequences from Homo sapiens. 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 Page seeded by OCA on Sat May 3 21:47:35 2008

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