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4ubf

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<StructureSection load='4ubf' size='340' side='right' caption='[[4ubf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='4ubf' size='340' side='right' caption='[[4ubf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ubf]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UBF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ubf]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UBF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIF2C, KNSL6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ubf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ubf OCA], [http://pdbe.org/4ubf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ubf RCSB], [http://www.ebi.ac.uk/pdbsum/4ubf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ubf ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ubf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ubf OCA], [http://pdbe.org/4ubf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ubf RCSB], [http://www.ebi.ac.uk/pdbsum/4ubf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ubf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KIF2C_HUMAN KIF2C_HUMAN]] In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis.<ref>PMID:19060894</ref> <ref>PMID:21820309</ref>
[[http://www.uniprot.org/uniprot/KIF2C_HUMAN KIF2C_HUMAN]] In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis.<ref>PMID:19060894</ref> <ref>PMID:21820309</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The precise regulation of microtubule dynamics is essential during cell division. The kinesin-13 motor protein MCAK is a potent microtubule depolymerase. The divergent non-motor regions flanking the ATPase domain are critical in regulating its targeting and activity. However, the molecular basis for the function of the non-motor regions within the context of full-length MCAK is unknown. Here, we determine the structure of MCAK motor domain bound to its regulatory C-terminus. Our analysis reveals that the MCAK C-terminus binds to two motor domains in solution and is displaced allosterically upon microtubule binding, which allows its robust accumulation at microtubule ends. These results demonstrate that MCAK undergoes long-range conformational changes involving its C-terminus during the soluble to microtubule-bound transition and that the C-terminus-motor interaction represents a structural intermediate in the MCAK catalytic cycle. Together, our work reveals intrinsic molecular mechanisms underlying the regulation of kinesin-13 activity.
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The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch.,Talapatra SK, Harker B, Welburn JP Elife. 2015 Apr 27;4. doi: 10.7554/eLife.06421. PMID:25915621<ref>PMID:25915621</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 4ubf" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Kinesin|Kinesin]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Human]]
[[Category: Talapatra, S K]]
[[Category: Talapatra, S K]]
[[Category: Welburn, J P.I]]
[[Category: Welburn, J P.I]]

Revision as of 06:08, 6 June 2018

HsMCAK motor domain complex

4ubf, resolution 3.00Å

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