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| - | {{Seed}} | |
| - | [[Image:3lre.jpg|left|200px]] | |
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| - | <!-- | + | ==Crystal Structure Analysis of Human Kinesin-8 Motor Domain== |
| - | The line below this paragraph, containing "STRUCTURE_3lre", creates the "Structure Box" on the page.
| + | <StructureSection load='3lre' size='340' side='right'caption='[[3lre]], [[Resolution|resolution]] 2.20Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3lre]] 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=3LRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LRE FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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> |
| - | {{STRUCTURE_3lre| PDB=3lre | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lre OCA], [https://pdbe.org/3lre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lre RCSB], [https://www.ebi.ac.uk/pdbsum/3lre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lre ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KI18A_HUMAN KI18A_HUMAN] Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression.<ref>PMID:17346968</ref> <ref>PMID:18267093</ref> <ref>PMID:18513970</ref> <ref>PMID:19625775</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Members of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse how kinesin-8 multitasks, we studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate the structure of the microtubule-bound motor. Microtubule-bound kinesin-8 reveals a new conformation compared with the crystal structure, including a bent conformation of the alpha4 relay helix and ordering of functionally important loops. The kinesin-8 motor domain does not depolymerise stabilised microtubules with ATP but does form tubulin rings in the presence of a non-hydrolysable ATP analogue. This shows that, by collaborating, kinesin-8 motor domain molecules can release tubulin from microtubules, and that they have a similar mechanical effect on microtubule ends as kinesin-13, which enables depolymerisation. Our data reveal aspects of the molecular mechanism of kinesin-8 motors that contribute to their unique dual motile and depolymerising functions, which are adapted to control microtubule length. |
| | | | |
| - | ===Crystal Structure Analysis of Human Kinesin-8 Motor Domain===
| + | Insight into the molecular mechanism of the multitasking kinesin-8 motor.,Peters C, Brejc K, Belmont L, Bodey AJ, Lee Y, Yu M, Guo J, Sakowicz R, Hartman J, Moores CA EMBO J. 2010 Oct 20;29(20):3437-47. Epub 2010 Sep 3. PMID:20818331<ref>PMID:20818331</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 3lre" style="background-color:#fffaf0;"></div> |
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| - | <!--
| + | ==See Also== |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_20818331}}, adds the Publication Abstract to the page
| + | *[[Kinesin 3D Structures|Kinesin 3D Structures]] |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 20818331 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_20818331}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | |
| - | 3LRE is a 2 chains structure with sequences 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=3LRE OCA].
| + | |
| - | | + | |
| - | ==Reference== | + | |
| - | <ref group="xtra">PMID:20818331</ref><references group="xtra"/> | + | |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Brejc, K.]] | + | [[Category: Large Structures]] |
| - | [[Category: Hartman, J.]] | + | [[Category: Brejc K]] |
| - | [[Category: Moores, C A.]] | + | [[Category: Hartman J]] |
| - | [[Category: Atp-binding]] | + | [[Category: Moores CA]] |
| - | [[Category: Cell projection]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Microtubule]]
| + | |
| - | [[Category: Microtubule binding]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 10 06:48:19 2010''
| + | |
| Structural highlights
Function
KI18A_HUMAN Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression.[1] [2] [3] [4]
Publication Abstract from PubMed
Members of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse how kinesin-8 multitasks, we studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate the structure of the microtubule-bound motor. Microtubule-bound kinesin-8 reveals a new conformation compared with the crystal structure, including a bent conformation of the alpha4 relay helix and ordering of functionally important loops. The kinesin-8 motor domain does not depolymerise stabilised microtubules with ATP but does form tubulin rings in the presence of a non-hydrolysable ATP analogue. This shows that, by collaborating, kinesin-8 motor domain molecules can release tubulin from microtubules, and that they have a similar mechanical effect on microtubule ends as kinesin-13, which enables depolymerisation. Our data reveal aspects of the molecular mechanism of kinesin-8 motors that contribute to their unique dual motile and depolymerising functions, which are adapted to control microtubule length.
Insight into the molecular mechanism of the multitasking kinesin-8 motor.,Peters C, Brejc K, Belmont L, Bodey AJ, Lee Y, Yu M, Guo J, Sakowicz R, Hartman J, Moores CA EMBO J. 2010 Oct 20;29(20):3437-47. Epub 2010 Sep 3. PMID:20818331[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mayr MI, Hummer S, Bormann J, Gruner T, Adio S, Woehlke G, Mayer TU. The human kinesin Kif18A is a motile microtubule depolymerase essential for chromosome congression. Curr Biol. 2007 Mar 20;17(6):488-98. Epub 2007 Mar 8. PMID:17346968 doi:10.1016/j.cub.2007.02.036
- ↑ Stumpff J, von Dassow G, Wagenbach M, Asbury C, Wordeman L. The kinesin-8 motor Kif18A suppresses kinetochore movements to control mitotic chromosome alignment. Dev Cell. 2008 Feb;14(2):252-62. doi: 10.1016/j.devcel.2007.11.014. PMID:18267093 doi:10.1016/j.devcel.2007.11.014
- ↑ Gardner MK, Odde DJ, Bloom K. Kinesin-8 molecular motors: putting the brakes on chromosome oscillations. Trends Cell Biol. 2008 Jul;18(7):307-10. doi: 10.1016/j.tcb.2008.05.003. Epub, 2008 May 29. PMID:18513970 doi:10.1016/j.tcb.2008.05.003
- ↑ Huang Y, Yao Y, Xu HZ, Wang ZG, Lu L, Dai W. Defects in chromosome congression and mitotic progression in KIF18A-deficient cells are partly mediated through impaired functions of CENP-E. Cell Cycle. 2009 Aug 15;8(16):2643-9. Epub 2009 Aug 29. PMID:19625775
- ↑ Peters C, Brejc K, Belmont L, Bodey AJ, Lee Y, Yu M, Guo J, Sakowicz R, Hartman J, Moores CA. Insight into the molecular mechanism of the multitasking kinesin-8 motor. EMBO J. 2010 Oct 20;29(20):3437-47. Epub 2010 Sep 3. PMID:20818331 doi:10.1038/emboj.2010.220
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