2vpv

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{{Seed}}
 
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[[Image:2vpv.png|left|200px]]
 
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==Dimerization Domain of Mif2p==
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The line below this paragraph, containing "STRUCTURE_2vpv", creates the "Structure Box" on the page.
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<StructureSection load='2vpv' size='340' side='right'caption='[[2vpv]], [[Resolution|resolution]] 2.70&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'>[[2vpv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VPV 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]] 2.7&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2vpv| PDB=2vpv | 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=2vpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vpv OCA], [https://pdbe.org/2vpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vpv RCSB], [https://www.ebi.ac.uk/pdbsum/2vpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vpv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CENPC_YEAST CENPC_YEAST] Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly (PubMed:8408221, PubMed:7579695, PubMed:22561346).<ref>PMID:22561346</ref> <ref>PMID:7579695</ref> <ref>PMID:8408221</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/vp/2vpv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2vpv 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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Mif2p is the budding-yeast orthologue of the mammalian centromere-binding protein CENP-C. We have mapped domains of Saccharomyces cerevisiae Mif2p and studied the phenotyptic consequences of their deletion. Using chromatin immunoprecipitation (ChIP) and electrophoretic mobility shift assays, we have further shown that Mif2p binds in the CDEIII region of the budding-yeast centromere, probably in close spatial association with Ndc10p. Moreover, ChIP experiments show that Mif2p recruits to yeast kinetochores a substantial subset of inner and outer kinetochore proteins, but not the Ndc80 or Spc105 complexes. We have determined the crystal structure of the C-terminal, dimerization domain of Mif2p. It has a "cupin" fold, extremely similar both in polypeptide chain conformation and in dimer geometry to the dimerization domain of a bacterial transcription factor. The Mif2p dimer seems to be part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast.
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===DIMERIZATION DOMAIN OF MIF2P===
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Structural and functional dissection of Mif2p, a conserved DNA-binding kinetochore protein.,Cohen RL, Espelin CW, De Wulf P, Sorger PK, Harrison SC, Simons KT Mol Biol Cell. 2008 Oct;19(10):4480-91. Epub 2008 Aug 13. PMID:18701705<ref>PMID:18701705</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_18701705}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2vpv" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18701705 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18701705}}
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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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2VPV is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VPV OCA].
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==Reference==
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<ref group="xtra">PMID:18701705</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Cohen, R L.]]
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[[Category: Cohen RL]]
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[[Category: Espelin, C W.]]
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[[Category: Espelin CW]]
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[[Category: Harrison, S C.]]
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[[Category: Harrison SC]]
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[[Category: Simons, K T.]]
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[[Category: Simons KT]]
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[[Category: Sorger, P K.]]
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[[Category: Sorger PK]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Centromere]]
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[[Category: Dimerization domain]]
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[[Category: Dna-binding]]
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[[Category: Jelly-roll fold]]
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[[Category: Kinetochore]]
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[[Category: Mitosis]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 22:39:56 2009''
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Current revision

Dimerization Domain of Mif2p

PDB ID 2vpv

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OCA

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