4ubf
From Proteopedia
(Difference between revisions)
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<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/ ] 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 [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> | ||
| + | <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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4ubf" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Kinesin|Kinesin]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| + | [[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
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Categories: Homo sapiens | Human | Talapatra, S K | Welburn, J P.I | Cell cycle | Complex | Kif2c | Mcak | Motor domain
