1uj2

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[[Image:1uj2.png|left|200px]]
 
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==Crystal structure of human uridine-cytidine kinase 2 complexed with products, CMP and ADP==
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The line below this paragraph, containing "STRUCTURE_1uj2", creates the "Structure Box" on the page.
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<StructureSection load='1uj2' size='340' side='right'caption='[[1uj2]], [[Resolution|resolution]] 1.80&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'>[[1uj2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UJ2 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]] 1.8&#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=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_1uj2| PDB=1uj2 | 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=1uj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uj2 OCA], [https://pdbe.org/1uj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uj2 RCSB], [https://www.ebi.ac.uk/pdbsum/1uj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uj2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UCK2_HUMAN UCK2_HUMAN] Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.
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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/uj/1uj2_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=1uj2 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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Uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine and cytidine and activates pharmacological ribonucleoside analogs. Here we present the crystal structures of human UCK alone and in complexes with a substrate, cytidine, a feedback inhibitor, CTP or UTP, and with phosphorylation products, CMP and ADP, respectively. Free UCK takes an alpha/beta mononucleotide binding fold and exists as a homotetramer with 222 symmetry. Upon inhibitor binding, one loop region was loosened, causing the UCK tetramer to be distorted. Upon cytidine binding, a large induced fit was observed at the uridine/cytidine binding site, which endows UCK with a strict specificity for pyrimidine ribonucleosides. The first UCK structure provided the structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase, which give clues for the design of novel antitumor and antiviral ribonucleoside analogs that inhibit RNA synthesis.
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===Crystal structure of human uridine-cytidine kinase 2 complexed with products, CMP and ADP===
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Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase.,Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F Structure. 2004 May;12(5):751-64. PMID:15130468<ref>PMID:15130468</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_15130468}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1uj2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15130468 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15130468}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1uj2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJ2 OCA].
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==Reference==
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<ref group="xtra">PMID:15130468</ref><ref group="xtra">PMID:12876357</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Uridine kinase]]
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[[Category: Large Structures]]
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[[Category: Fukushima, M.]]
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[[Category: Fukushima M]]
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[[Category: Inagaki, F.]]
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[[Category: Inagaki F]]
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[[Category: Koizumi, K.]]
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[[Category: Koizumi K]]
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[[Category: Matsuda, A.]]
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[[Category: Matsuda A]]
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[[Category: Suzuki, N N.]]
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[[Category: Suzuki NN]]
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[[Category: Alpha/beta mononucleotide-binding hold]]
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[[Category: Transferase]]
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Current revision

Crystal structure of human uridine-cytidine kinase 2 complexed with products, CMP and ADP

PDB ID 1uj2

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