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2rkp

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{{STRUCTURE_2rkp| PDB=2rkp | SCENE= }}
{{STRUCTURE_2rkp| PDB=2rkp | SCENE= }}
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'''Crystal structure of the catalytic subunit of human protein kinase CK2 with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole'''
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===Crystal structure of the catalytic subunit of human protein kinase CK2 with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole===
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==Overview==
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The Ser/Thr kinase CK2 (previously called casein kinase 2) is composed of two catalytic chains (CK2alpha) attached to a dimer of noncatalytic subunits (CK2beta). CK2 is involved in suppression of apoptosis, cell survival, and tumorigenesis. To investigate these activities and possibly affect them, selective CK2 inhibitors are required. An often-used CK2 inhibitor is 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB). In a complex structure with human CK2alpha, DRB binds to the canonical ATP cleft, but additionally it occupies an allosteric site that can be alternatively filled by glycerol. Inhibition kinetic studies corroborate the dual binding mode of the inhibitor. Structural comparisons reveal a surprising conformational plasticity of human CK2alpha around both DRB binding sites. After local rearrangement, the allosteric site serves as a CK2beta interface. This opens the potential to construct molecules interfering with the CK2alpha/CK2beta interaction.
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(as it appears on PubMed at http://www.pubmed.gov), where 18291315 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18291315}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The CK2alpha/CK2beta Interface of Human Protein Kinase CK2 Harbors a Binding Pocket for Small Molecules., Raaf J, Brunstein E, Issinger OG, Niefind K, Chem Biol. 2008 Feb;15(2):111-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18291315 18291315]
The CK2alpha/CK2beta Interface of Human Protein Kinase CK2 Harbors a Binding Pocket for Small Molecules., Raaf J, Brunstein E, Issinger OG, Niefind K, Chem Biol. 2008 Feb;15(2):111-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18291315 18291315]
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Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases., Niefind K, Yde CW, Ermakova I, Issinger OG, J Mol Biol. 2007 Jul 13;370(3):427-38. Epub 2007 May 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17524418 17524418]
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Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit., Ermakova I, Boldyreff B, Issinger OG, Niefind K, J Mol Biol. 2003 Jul 25;330(5):925-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12860116 12860116]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Wnt signaling pathway]]
[[Category: Wnt signaling pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:05:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:09:20 2008''

Revision as of 03:09, 28 July 2008

Image:2rkp.png

Template:STRUCTURE 2rkp

Crystal structure of the catalytic subunit of human protein kinase CK2 with 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole

Template:ABSTRACT PUBMED 18291315

About this Structure

2RKP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The CK2alpha/CK2beta Interface of Human Protein Kinase CK2 Harbors a Binding Pocket for Small Molecules., Raaf J, Brunstein E, Issinger OG, Niefind K, Chem Biol. 2008 Feb;15(2):111-7. PMID:18291315

Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases., Niefind K, Yde CW, Ermakova I, Issinger OG, J Mol Biol. 2007 Jul 13;370(3):427-38. Epub 2007 May 5. PMID:17524418

Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit., Ermakova I, Boldyreff B, Issinger OG, Niefind K, J Mol Biol. 2003 Jul 25;330(5):925-34. PMID:12860116

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