3bw5

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{{STRUCTURE_3bw5| PDB=3bw5 | SCENE= }}
{{STRUCTURE_3bw5| PDB=3bw5 | SCENE= }}
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'''Crystal structure of a mutant of human protein kinase CK2alpha with altered cosubstrate specificity'''
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===Crystal structure of a mutant of human protein kinase CK2alpha with altered cosubstrate specificity===
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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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The line below this paragraph, {{ABSTRACT_PUBMED_18291315}}, adds the Publication Abstract to the page
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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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Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate., Yde CW, Ermakova I, Issinger OG, Niefind K, J Mol Biol. 2005 Mar 25;347(2):399-414. Epub 2005 Jan 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15740749 15740749]
[[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 21:09:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:42:58 2008''

Revision as of 06:42, 28 July 2008

Image:3bw5.png

Template:STRUCTURE 3bw5

Crystal structure of a mutant of human protein kinase CK2alpha with altered cosubstrate specificity

Template:ABSTRACT PUBMED 18291315

About this Structure

3BW5 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1ymi. 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

Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate., Yde CW, Ermakova I, Issinger OG, Niefind K, J Mol Biol. 2005 Mar 25;347(2):399-414. Epub 2005 Jan 18. PMID:15740749

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