1p62

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[[Image:1p62.jpg|left|200px]]
 
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==Structure of human dCK complexed with gemcitabine and ADP-MG==
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The line below this paragraph, containing "STRUCTURE_1p62", creates the "Structure Box" on the page.
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<StructureSection load='1p62' size='340' side='right'caption='[[1p62]], [[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'>[[1p62]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P62 FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GEO:GEMCITABINE'>GEO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1p62| PDB=1p62 | SCENE= }}
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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=1p62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p62 OCA], [https://pdbe.org/1p62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p62 RCSB], [https://www.ebi.ac.uk/pdbsum/1p62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p62 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DCK_HUMAN DCK_HUMAN] Required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA). Has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. It is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents.<ref>PMID:18377927</ref> <ref>PMID:20614893</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/p6/1p62_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=1p62 ConSurf].
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<div style="clear:both"></div>
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'''Structure of human dCK complexed with gemcitabine and ADP-MG'''
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==See Also==
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*[[Deoxycytidine kinase 3D structures|Deoxycytidine kinase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Human deoxycytidine kinase (dCK) phosphorylates the natural deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG) and deoxyadenosine (dA) and is an essential enzyme for the phosphorylation of numerous nucleoside analog prodrugs routinely used in cancer and antiviral chemotherapy. For many of these compounds, the phosphorylation step catalyzed by dCK is the rate-limiting step in their overall activation pathway. To determine the factors that limit the phosphorylation efficiency of the prodrug, we solved the crystal structure of dCK to a resolution of 1.6 A in complex with its physiological substrate deoxycytidine and with the prodrugs AraC and gemcitabine. The structures reveal the determinants of dCK substrate specificity. Especially relevant to new prodrug development is the interaction between Arg128 and the hydrogen-bond acceptor at the sugar 2'-arabinosyl position of AraC and gemcitabine. On the basis of the structures, we designed a catalytically superior dCK variant that could be used in suicide gene-therapy applications.
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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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1P62 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P62 OCA].
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==Reference==
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Structure of human dCK suggests strategies to improve anticancer and antiviral therapy., Sabini E, Ort S, Monnerjahn C, Konrad M, Lavie A, Nat Struct Biol. 2003 Jul;10(7):513-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12808445 12808445]
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[[Category: Deoxycytidine kinase]]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Konrad M]]
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[[Category: Konrad, M.]]
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[[Category: Lavie A]]
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[[Category: Lavie, A.]]
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[[Category: Monnerjahn C]]
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[[Category: Monnerjahn, C.]]
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[[Category: Ort S]]
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[[Category: Ort, S.]]
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[[Category: Sabini E]]
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[[Category: Sabini, E.]]
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[[Category: Gemcitabine]]
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[[Category: Nucleoside kinase]]
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[[Category: P-loop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:43:53 2008''
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Current revision

Structure of human dCK complexed with gemcitabine and ADP-MG

PDB ID 1p62

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