1ob3

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{{Seed}}
 
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[[Image:1ob3.png|left|200px]]
 
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==Structure of P. falciparum PfPK5==
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The line below this paragraph, containing "STRUCTURE_1ob3", creates the "Structure Box" on the page.
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<StructureSection load='1ob3' size='340' side='right'caption='[[1ob3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ob3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OB3 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ob3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ob3 OCA], [https://pdbe.org/1ob3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ob3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ob3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ob3 ProSAT]</span></td></tr>
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{{STRUCTURE_1ob3| PDB=1ob3 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDK2H_PLAFK CDK2H_PLAFK] Serine/threonine-protein kinase (PubMed:8844681, PubMed:14604523). Involved in the control of the cell cycle (By similarity). Required for entry into S-phase and mitosis (By similarity). Probable component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity). In schizonts, phosphorylates ORC1 resulting in its dissociation from DNA, relocalization to the cytoplasm and likely its degradation (By similarity).[UniProtKB:P04551]<ref>PMID:14604523</ref> <ref>PMID:8844681</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ob/1ob3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ob3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===STRUCTURE OF P. FALCIPARUM PFPK5===
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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<ref>PMID:14604523</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14604523}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ob3" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14604523 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14604523}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1OB3 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OB3 OCA].
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==Reference==
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<ref group="xtra">PMID:14604523</ref><references group="xtra"/>
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[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
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[[Category: Burgess, D.]]
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[[Category: Burgess D]]
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[[Category: Doerig, C.]]
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[[Category: Doerig C]]
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[[Category: Endicott, J.]]
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[[Category: Endicott J]]
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[[Category: Holton, S.]]
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[[Category: Holton S]]
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[[Category: Merckx, A.]]
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[[Category: Merckx A]]
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[[Category: Noble, M.]]
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[[Category: Noble M]]
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[[Category: Atp-binding]]
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[[Category: Cdk]]
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[[Category: Phosphorylation]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 21:05:30 2009''
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Current revision

Structure of P. falciparum PfPK5

PDB ID 1ob3

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OCA

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