1t5c

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[[Image:1t5c.gif|left|200px]]
 
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{{Structure
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==Crystal structure of the motor domain of human kinetochore protein CENP-E==
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|PDB= 1t5c |SIZE=350|CAPTION= <scene name='initialview01'>1t5c</scene>, resolution 2.5&Aring;
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<StructureSection load='1t5c' size='340' side='right'caption='[[1t5c]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=PIN:PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)'>PIN</scene>
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<table><tr><td colspan='2'>[[1t5c]] 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=1T5C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T5C FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.5&#8491;</td></tr>
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|GENE= CENPE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PIN:PIPERAZINE-N,N-BIS(2-ETHANESULFONIC+ACID)'>PIN</scene></td></tr>
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}}
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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=1t5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t5c OCA], [https://pdbe.org/1t5c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t5c RCSB], [https://www.ebi.ac.uk/pdbsum/1t5c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t5c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CENPE_HUMAN CENPE_HUMAN] Essential for the maintenance of chromosomal stability through efficient stabilization of microtubule capture at kinetochores. Plays a key role in the movement of chromosomes toward the metaphase plate during mitosis. Is a slow plus end-directed motor whose activity is essential for metaphase chromosome alignment. Couples chromosome position to microtubule depolymerizing activity. The highly processive microtubule-dependent motor activity of CENPE serves to power chromosome congression and provides a flexible, motile tether linking kinetochores to dynamic spindle microtubules. Necessary for the mitotic checkpoint signal at individual kinetochores to prevent aneuploidy due to single chromosome loss. Required for the efficient recruitment of BUBR1, MAD1 and MAD2 to attached and newly unattached kinetochores. Stimulates mammalian BUBR1 kinase activity. Accumulates just before mitosis at the G2 phase of the cell cycle.<ref>PMID:7889940</ref> <ref>PMID:17535814</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/t5/1t5c_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=1t5c 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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The human kinetochore is a highly complex macromolecular structure that connects chromosomes to spindle microtubules (MTs) in order to facilitate accurate chromosome segregation. Centromere-associated protein E (CENP-E), a member of the kinesin superfamily, is an essential component of the kinetochore, since it is required to stabilize the attachment of chromosomes to spindle MTs, to develop tension across aligned chromosomes, to stabilize spindle poles and to satisfy the mitotic checkpoint. Here we report the 2.5A resolution crystal structure of the motor domain and linker region of human CENP-E with MgADP bound in the active site. This structure displays subtle but important differences compared to the structures of human Eg5 and conventional kinesin. Our structure reveals that the CENP-E linker region is in a "docked" position identical to that in the human plus-end directed conventional kinesin. CENP-E has many advantages as a potential anti-mitotic drug target and this crystal structure of human CENP-E will provide a starting point for high throughput virtual screening of potential inhibitors.
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'''Crystal structure of the motor domain of human kinetochore protein CENP-E'''
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Crystal structure of the motor domain of the human kinetochore protein CENP-E.,Garcia-Saez I, Yen T, Wade RH, Kozielski F J Mol Biol. 2004 Jul 23;340(5):1107-16. PMID:15236970<ref>PMID:15236970</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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<div class="pdbe-citations 1t5c" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The human kinetochore is a highly complex macromolecular structure that connects chromosomes to spindle microtubules (MTs) in order to facilitate accurate chromosome segregation. Centromere-associated protein E (CENP-E), a member of the kinesin superfamily, is an essential component of the kinetochore, since it is required to stabilize the attachment of chromosomes to spindle MTs, to develop tension across aligned chromosomes, to stabilize spindle poles and to satisfy the mitotic checkpoint. Here we report the 2.5A resolution crystal structure of the motor domain and linker region of human CENP-E with MgADP bound in the active site. This structure displays subtle but important differences compared to the structures of human Eg5 and conventional kinesin. Our structure reveals that the CENP-E linker region is in a "docked" position identical to that in the human plus-end directed conventional kinesin. CENP-E has many advantages as a potential anti-mitotic drug target and this crystal structure of human CENP-E will provide a starting point for high throughput virtual screening of potential inhibitors.
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*[[Centromere protein 3D structure|Centromere protein 3D structure]]
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== References ==
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==About this Structure==
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<references/>
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1T5C is a [[Single protein]] structure of 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=1T5C OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of the motor domain of the human kinetochore protein CENP-E., Garcia-Saez I, Yen T, Wade RH, Kozielski F, J Mol Biol. 2004 Jul 23;340(5):1107-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15236970 15236970]
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[[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: Garcia-Saez, I.]]
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[[Category: Garcia-Saez I]]
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[[Category: Kozielski, F.]]
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[[Category: Kozielski F]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: Wade RH]]
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[[Category: Wade, R H.]]
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[[Category: Yen T]]
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[[Category: Yen, T.]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: NO3]]
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[[Category: PIN]]
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[[Category: arrow-head shape]]
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[[Category: kinesin motor-domain-adp complex]]
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[[Category: spine]]
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[[Category: stranded beta-sheet core with solvent exposed alpha-helice]]
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[[Category: structural genomic]]
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[[Category: structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:14:00 2008''
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Current revision

Crystal structure of the motor domain of human kinetochore protein CENP-E

PDB ID 1t5c

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