1m2q: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MNX:1,8-DI-HYDROXY-4-NITRO-XANTHEN-9-ONE'>MNX</scene> | |LIGAND= <scene name='pdbligand=MNX:1,8-DI-HYDROXY-4-NITRO-XANTHEN-9-ONE'>MNX</scene> | ||
|ACTIVITY= [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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1j91|1J91]], [[1jam|1JAM]], [[1f0q|1F0Q]], [[1m2p|1M2P]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2q OCA], [http://www.ebi.ac.uk/pdbsum/1m2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m2q RCSB]</span> | |||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Zagotto, G.]] | [[Category: Zagotto, G.]] | ||
[[Category: Zanotti, G.]] | [[Category: Zanotti, G.]] | ||
[[Category: inhibitor-enzyme complex]] | [[Category: inhibitor-enzyme complex]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:10:33 2008'' | ||
Revision as of 22:10, 30 March 2008
| |||||||
| , resolution 1.79Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Related: | 1J91, 1JAM, 1F0Q, 1M2P
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of 1,8-di-hydroxy-4-nitro-xanten-9-one/CK2 kinase complex
OverviewOverview
Protein kinases play key roles in signal transduction and therefore are among the most attractive targets for drug design. The pharmacological aptitude of protein kinase inhibitors is highlighted by the observation that various diseases with special reference to cancer are because of the abnormal expression/activity of individual kinases. The resolution of the three-dimensional structure of the target kinase in complex with inhibitors is often the starting point for the rational design of this kind of drugs, some of which are already in advanced clinical trial or even in clinical practice. Here we present and discuss three new crystal structures of ATP site-directed inhibitors in complex with "casein kinase-2" (CK2), a constitutively active protein kinase implicated in a variety of cellular functions and misfunctions. With the help of theoretical calculations, we disclose some key features underlying the inhibitory efficiency of anthraquinone derivatives, outlining three different binding modes into the active site. In particular, we show that a nitro group in a hydroxyanthraquinone scaffold decreases the inhibitory constants K(i) because of electron-withdrawing and resonance effects that enhance the polarization of hydroxylic substituents in paraposition.
About this StructureAbout this Structure
1M2Q is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.
ReferenceReference
Inhibition of protein kinase CK2 by anthraquinone-related compounds. A structural insight., De Moliner E, Moro S, Sarno S, Zagotto G, Zanotti G, Pinna LA, Battistutta R, J Biol Chem. 2003 Jan 17;278(3):1831-6. Epub 2002 Nov 4. PMID:12419810
Page seeded by OCA on Sun Mar 30 22:10:33 2008