1uj2

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(New page: 200px<br /> <applet load="1uj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uj2, resolution 1.80&Aring;" /> '''Crystal structure o...)
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[[Image:1uj2.gif|left|200px]]<br />
 
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<applet load="1uj2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1uj2, resolution 1.80&Aring;" />
 
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'''Crystal structure of human uridine-cytidine kinase 2 complexed with products, CMP and ADP'''<br />
 
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==Overview==
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==Crystal structure of human uridine-cytidine kinase 2 complexed with products, CMP and ADP==
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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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<StructureSection load='1uj2' size='340' side='right'caption='[[1uj2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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==About this Structure==
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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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1UJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, C5P and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Uridine_kinase Uridine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.48 2.7.1.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UJ2 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15130468 15130468]
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</div>
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<div class="pdbe-citations 1uj2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Uridine kinase]]
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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 NN]]
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[[Category: Suzuki, N.N.]]
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[[Category: ADP]]
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[[Category: C5P]]
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[[Category: MG]]
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[[Category: alpha/beta mononucleotide-binding hold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:35:28 2007''
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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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