2oxx: Difference between revisions
New page: left|200px<br /><applet load="2oxx" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oxx, resolution 2.30Å" /> '''Protein kinase CK2 i... |
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==Overview== | ==Overview== | ||
CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote | CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote cell survival and enhance the tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K(i) values between 0.15 and 0.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, in an area with a positive electrostatic potential that is able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining the ligand orientation and binding selectivity. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
The ATP- | The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules., Battistutta R, Mazzorana M, Cendron L, Bortolato A, Sarno S, Kazimierczuk Z, Zanotti G, Moro S, Pinna LA, Chembiochem. 2007 Oct 15;8(15):1804-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17768728 17768728] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:23:48 2008'' | ||
Revision as of 19:23, 21 February 2008
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Protein kinase CK2 in complex with tetrabromobenzoimidazole derivatives K17, K22 and K32
OverviewOverview
CK2 is a highly pleiotropic Ser/Thr protein kinase that is able to promote cell survival and enhance the tumour phenotype under specific circumstances. We have determined the crystal structure of three new complexes with tetrabromobenzimidazole derivatives that display K(i) values between 0.15 and 0.30 microM. A comparative analysis of these data with those of four other inhibitors of the same family revealed the presence of some highly conserved water molecules in the ATP-binding site. These waters reside near Lys68, in an area with a positive electrostatic potential that is able to attract and orient negatively charged ligands. The presence of this positive region and two unique bulky residues that are typical of CK2, Ile66 and Ile174, play a critical role in determining the ligand orientation and binding selectivity.
About this StructureAbout this Structure
2OXX is a Single protein structure of sequence from Zea mays with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
ReferenceReference
The ATP-binding site of protein kinase CK2 holds a positive electrostatic area and conserved water molecules., Battistutta R, Mazzorana M, Cendron L, Bortolato A, Sarno S, Kazimierczuk Z, Zanotti G, Moro S, Pinna LA, Chembiochem. 2007 Oct 15;8(15):1804-9. PMID:17768728
Page seeded by OCA on Thu Feb 21 18:23:48 2008