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| | ==HsMCAK motor domain complex== | | ==HsMCAK motor domain complex== |
| - | <StructureSection load='4ubf' size='340' side='right' caption='[[4ubf]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4ubf' size='340' side='right'caption='[[4ubf]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <table><tr><td colspan='2'>[[4ubf]] is a 5 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=4UBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <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'>[https://proteopedia.org/fgij/fg.htm?mol=4ubf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ubf OCA], [https://pdbe.org/4ubf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ubf RCSB], [https://www.ebi.ac.uk/pdbsum/4ubf PDBsum], [https://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> | + | [https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Kinesin|Kinesin]] | + | *[[Kinesin 3D Structures|Kinesin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Talapatra, S K]] | + | [[Category: Talapatra SK]] |
| - | [[Category: Welburn, J P.I]] | + | [[Category: Welburn JPI]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Kif2c]]
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| - | [[Category: Mcak]]
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| - | [[Category: Motor domain]]
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| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bakhoum SF, Thompson SL, Manning AL, Compton DA. Genome stability is ensured by temporal control of kinetochore-microtubule dynamics. Nat Cell Biol. 2009 Jan;11(1):27-35. doi: 10.1038/ncb1809. Epub 2008 Dec 7. PMID:19060894 doi:http://dx.doi.org/10.1038/ncb1809
- ↑ Tanenbaum ME, Macurek L, van der Vaart B, Galli M, Akhmanova A, Medema RH. A complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinases. Curr Biol. 2011 Aug 23;21(16):1356-65. doi: 10.1016/j.cub.2011.07.017. Epub 2011 , Aug 4. PMID:21820309 doi:http://dx.doi.org/10.1016/j.cub.2011.07.017
- ↑ Talapatra SK, Harker B, Welburn JP. The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch. Elife. 2015 Apr 27;4. doi: 10.7554/eLife.06421. PMID:25915621 doi:http://dx.doi.org/10.7554/eLife.06421
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