4hna
From Proteopedia
(Difference between revisions)
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- | + | ==Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN== | |
- | + | <StructureSection load='4hna' size='340' side='right' caption='[[4hna]], [[Resolution|resolution]] 3.19Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[4hna]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alfaropsis_roxburghiana Alfaropsis roxburghiana], [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HNA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HNA 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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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">KIF5B, KNS, KNS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139932 Alfaropsis roxburghiana])</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=4hna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hna OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hna RCSB], [http://www.ebi.ac.uk/pdbsum/4hna PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to alphabeta-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken. | ||
- | + | Structure of a kinesin-tubulin complex and implications for kinesin motility.,Gigant B, Wang W, Dreier B, Jiang Q, Pecqueur L, Pluckthun A, Wang C, Knossow M Nat Struct Mol Biol. 2013 Aug;20(8):1001-7. doi: 10.1038/nsmb.2624. Epub 2013 Jul, 21. PMID:23872990<ref>PMID:23872990</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
==See Also== | ==See Also== | ||
+ | *[[Kinesin|Kinesin]] | ||
*[[Tubulin|Tubulin]] | *[[Tubulin|Tubulin]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Alfaropsis roxburghiana]] | [[Category: Alfaropsis roxburghiana]] | ||
[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
- | [[Category: Gigant, B | + | [[Category: Gigant, B]] |
- | [[Category: Knossow, M | + | [[Category: Knossow, M]] |
[[Category: Alpha-tubulin]] | [[Category: Alpha-tubulin]] | ||
[[Category: Beta-tubulin]] | [[Category: Beta-tubulin]] |
Revision as of 12:25, 21 December 2014
Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN
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