1v0o
From Proteopedia
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|PDB= 1v0o |SIZE=350|CAPTION= <scene name='initialview01'>1v0o</scene>, resolution 1.90Å | |PDB= 1v0o |SIZE=350|CAPTION= <scene name='initialview01'>1v0o</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=INA:Inr+Binding+Site+For+Chain+B'>INA</scene> | |SITE= <scene name='pdbsite=INA:Inr+Binding+Site+For+Chain+B'>INA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=INR:2',3-DIOXO-1,1',2',3-TETRAHYDRO-2,3'-BIINDOLE-5'-SULFONIC ACID'>INR</scene> | + | |LIGAND= <scene name='pdbligand=INR:2',3-DIOXO-1,1',2',3-TETRAHYDRO-2,3'-BIINDOLE-5'-SULFONIC+ACID'>INR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0o OCA], [http://www.ebi.ac.uk/pdbsum/1v0o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v0o RCSB]</span> | ||
}} | }} | ||
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[[Category: Merckx, A.]] | [[Category: Merckx, A.]] | ||
[[Category: Noble, M.]] | [[Category: Noble, M.]] | ||
| - | [[Category: INR]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
[[Category: cdk]] | [[Category: cdk]] | ||
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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 Mon Mar 31 00:17:59 2008'' |
Revision as of 21:18, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Sites: | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF P. FALCIPARUM PFPK5-INDIRUBIN-5-SULPHONATE LIGAND COMPLEX
Overview
Plasmodium falciparum cell cycle regulators are promising targets for antimalarial drug design. We have determined the structure of PfPK5, the first structure of a P. falciparum protein kinase and the first of a cyclin-dependent kinase (CDK) not derived from humans. The fold and the mechanism of inactivation of monomeric CDKs are highly conserved across evolution. ATP-competitive CDK inhibitors have been developed as potential leads for cancer therapeutics. These studies have identified regions of the CDK active site that can be exploited to achieve significant gains in inhibitor potency and selectivity. We have cocrystallized PfPK5 with three inhibitors that target such regions. The sequence differences between PfPK5 and human CDKs within these inhibitor binding sites suggest that selective inhibition is an attainable goal. Such compounds will be useful tools for P. falciparum cell cycle studies, and will provide lead compounds for antimalarial drug development.
About this Structure
1V0O is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
Structures of P. falciparum PfPK5 test the CDK regulation paradigm and suggest mechanisms of small molecule inhibition., Holton S, Merckx A, Burgess D, Doerig C, Noble M, Endicott J, Structure. 2003 Nov;11(11):1329-37. PMID:14604523
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