2cn5
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
- | 2CN5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CL, MG, NO3 and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 2CN5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CL, MG, NO3 and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CN5 OCA]]. |
==Reference== | ==Reference== | ||
Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange., Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH, EMBO J. 2006 Jul 12;25(13):3179-90. Epub 2006 Jun 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16794575 16794575] | Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange., Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH, EMBO J. 2006 Jul 12;25(13):3179-90. Epub 2006 Jun 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16794575 16794575] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
+ | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Oliver, A.W.]] | [[Category: Oliver, A.W.]] | ||
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[[Category: tumour suppressor]] | [[Category: tumour suppressor]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:08:13 2007'' |
Revision as of 08:03, 30 October 2007
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CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH ADP
Overview
The protein kinase Chk2 (checkpoint kinase 2) is a major effector of the, replication checkpoint. Chk2 activation is initiated by phosphorylation of, Thr68, in the serine-glutamine/threonine-glutamine cluster domain (SCD), by ATM. The phosphorylated SCD-segment binds to the FHA domain of a second, Chk2 molecule, promoting dimerisation of the protein and triggering, phosphorylation of the activation segment/T-loop in the kinase domain. We, have now determined the structure of the kinase domain of human Chk2 in, complexes with ADP and a small-molecule inhibitor debromohymenialdisine., The structure reveals a remarkable dimeric arrangement in which T-loops, are exchanged between protomers, to form an active kinase conformation in, trans. Biochemical data suggest that this dimer is the ... [(full description)]
About this Structure
2CN5 is a [Single protein] structure of sequence from [Homo sapiens] with CL, MG, NO3 and ADP as [ligands]. Active as [Non-specific serine/threonine protein kinase], with EC number [2.7.11.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange., Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH, EMBO J. 2006 Jul 12;25(13):3179-90. Epub 2006 Jun 22. PMID:16794575
Page seeded by OCA on Tue Oct 30 10:08:13 2007
Categories: Homo sapiens | Non-specific serine/threonine protein kinase | Single protein | Oliver, A.W. | Pearl, L.H. | ADP | CL | MG | NO3 | Activation segment | Alternative splicing | Atp-binding | Cancer | Cds1 | Cell cycle | Checkpoint | Chek2 | Chk2 | Disease mutation | Kinase | Kinase domain | Li-fraumeni syndrome | Magnesium | Metal-binding | Nuclear protein | Nucleotide-binding | Phosphorylation | Proto-oncogene | Rad53 | Serine/threonine-protein kinase | Transferase | Tumour suppressor