2y5w
From Proteopedia
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| - | [[ | + | ==CRYSTAL STRUCTURE OF DROSOPHILA MELANOGASTER KINESIN-1 MOTOR DOMAIN DIMER== |
| + | <StructureSection load='2y5w' size='340' side='right' caption='[[2y5w]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2y5w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y5W 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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2y65|2y65]]</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=2y5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y5w RCSB], [http://www.ebi.ac.uk/pdbsum/2y5w PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | When not transporting cargo, kinesin-1 is autoinhibited by binding of a tail region to the motor domains, but the mechanism of inhibition is unclear. We report the crystal structure of a motor domain dimer in complex with its tail domain at 2.2 angstroms and compare it with a structure of the motor domain alone at 2.7 angstroms. These structures indicate that neither an induced conformational change nor steric blocking is the cause of inhibition. Instead, the tail cross-links the motor domains at a second position, in addition to the coiled coil. This "double lockdown," by cross-linking at two positions, prevents the movement of the motor domains that is needed to undock the neck linker and release adenosine diphosphate. This autoinhibition mechanism could extend to some other kinesins. | ||
| - | + | The structure of the kinesin-1 motor-tail complex reveals the mechanism of autoinhibition.,Kaan HY, Hackney DD, Kozielski F Science. 2011 Aug 12;333(6044):883-5. PMID:21836017<ref>PMID:21836017</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Kinesin|Kinesin]] | *[[Kinesin|Kinesin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Hackney, D D.]] | [[Category: Hackney, D D.]] | ||
Revision as of 12:49, 22 October 2014
CRYSTAL STRUCTURE OF DROSOPHILA MELANOGASTER KINESIN-1 MOTOR DOMAIN DIMER
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