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4ubf

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Revision as of 08:13, 22 March 2023

HsMCAK motor domain complex

Structural highlights

4ubf is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ubf"

Categories: Homo sapiens | Large Structures | Talapatra SK | Welburn JPI

@@ Line 1: / Line 1: @@
 ==HsMCAK motor domain complex==
-<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 ==
-<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>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 20: @@
 ==See Also==
-*[[Kinesin|Kinesin]]
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
 == References ==
 <references/>
@@ Line 27: / Line 26: @@
 </StructureSection>
 [[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]]
-[[Category: Mcak]]
-[[Category: Motor domain]]

4ubf

From Proteopedia

Revision as of 08:13, 22 March 2023

HsMCAK motor domain complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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