1nsk

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(New page: 200px<br /> <applet load="1nsk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nsk, resolution 2.8&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1nsk.gif|left|200px]]<br />
 
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<applet load="1nsk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nsk, resolution 2.8&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF A HUMAN NUCLEOSIDE DIPHOSPHATE KINASE, NM23-H2'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURE OF A HUMAN NUCLEOSIDE DIPHOSPHATE KINASE, NM23-H2==
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The 2.8 A resolution X-ray structure of NM23-H2 has been determined by, molecular replacement using the structure of Myxococcus xanthus nucleoside, diphosphate (NDP) kinase. NM23-H2 is a human NDP kinase. The enzyme, catalyses phosphoryl transfer, binds DNA, and can activate the, transcription of the c-myc oncogene in vitro. NM23 has also been reported, to be a suppressor of metastasis in some types of tumours. Whereas the M., xanthus NDP kinase is a tetramer, NM23-H2 is a hexamer. The fold of, NM23-H2 is identical to the fold of other NDP kinases. Two antiparallel, helices joined by a turn form one edge of the nucleotide binding cleft., This region moves in a hinge-like fashion in response to substrate binding, and crystal packing forces. Additional differences in conformation among, the NDP kinases are principally in regions involved in protein-protein, contacts within the oligomers. The only protein-protein interaction, conserved among all NDP kinases is a dimeric interaction. Several, mutations of NM23-H2 have been detected in tumour tissues. These mutations, do not involve residues interacting with the substrates, and probably, destabilise the enzyme without directly affecting the catalytic activity., Low level phosphorylation of serines has been reported for NM23 both in, vitro and in vivo. The structure of the hexamer indicates that two serine, residues that have been reported as being phosphorylated, Ser44 and, Ser122, are on the surface of the hexamer, and are likely to be, phosphorylated by exogenous kinases. In contrast, Ser120 is buried, and is, most likely phosphorylated by a direct transfer from the phosphohistidine, intermediate of the reaction mechanism.
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<StructureSection load='1nsk' size='340' side='right'caption='[[1nsk]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nsk]] is a 6 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=1NSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSK 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]] 2.8&#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=1nsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsk OCA], [https://pdbe.org/1nsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsk RCSB], [https://www.ebi.ac.uk/pdbsum/1nsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NDKB_HUMAN NDKB_HUMAN] Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity.<ref>PMID:15249197</ref> <ref>PMID:20946858</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/ns/1nsk_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=1nsk ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1NSK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NSK OCA].
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*[[Nucleoside diphosphate kinase 3D structures|Nucleoside diphosphate kinase 3D structures]]
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== References ==
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==Reference==
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<references/>
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The crystal structure of a human nucleoside diphosphate kinase, NM23-H2., Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL, J Mol Biol. 1995 Aug 25;251(4):574-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7658474 7658474]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Nucleoside-diphosphate kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Perisic O]]
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[[Category: Perisic, O.]]
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[[Category: Williams RL]]
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[[Category: Williams, R.L.]]
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[[Category: phosphotransferase (po4 as acceptor)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:24:57 2007''
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Current revision

THE CRYSTAL STRUCTURE OF A HUMAN NUCLEOSIDE DIPHOSPHATE KINASE, NM23-H2

PDB ID 1nsk

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