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2y5w
From Proteopedia
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| - | [[Image:2y5w.png|left|200px]] | ||
| - | + | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2Y5W FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5w OCA], [https://pdbe.org/2y5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y5w RCSB], [https://www.ebi.ac.uk/pdbsum/2y5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y5w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KINH_DROME KINH_DROME] | ||
| + | <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> | |
| - | + | <div class="pdbe-citations 2y5w" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Kinesin|Kinesin]] | + | *[[Kinesin 3D Structures|Kinesin 3D Structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Hackney DD]] |
| - | [[Category: | + | [[Category: Kaan HYK]] |
| - | [[Category: | + | [[Category: Kozielski F]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer
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