3j1t
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DYHC1_MOUSE DYHC1_MOUSE] Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. | [https://www.uniprot.org/uniprot/DYHC1_MOUSE DYHC1_MOUSE] Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cytoplasmic dynein is a microtubule-based motor required for intracellular transport and cell division. Its movement involves coupling cycles of track binding and release with cycles of force-generating nucleotide hydrolysis. How this is accomplished given the ~25 nanometers separating dynein's track- and nucleotide-binding sites is not understood. Here, we present a subnanometer-resolution structure of dynein's microtubule-binding domain bound to microtubules by cryo-electron microscopy that was used to generate a pseudo-atomic model of the complex with molecular dynamics. We identified large rearrangements triggered by track binding and specific interactions, confirmed by mutagenesis and single-molecule motility assays, which tune dynein's affinity for microtubules. Our results provide a molecular model for how dynein's binding to microtubules is communicated to the rest of the motor. | ||
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| - | Structural basis for microtubule binding and release by dynein.,Redwine WB, Hernandez-Lopez R, Zou S, Huang J, Reck-Peterson SL, Leschziner AE Science. 2012 Sep 21;337(6101):1532-6. PMID:22997337<ref>PMID:22997337</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3j1t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Dynein 3D structures|Dynein 3D structures]] | *[[Dynein 3D structures|Dynein 3D structures]] | ||
*[[Tubulin 3D Structures|Tubulin 3D Structures]] | *[[Tubulin 3D Structures|Tubulin 3D Structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
Current revision
High affinity dynein microtubule binding domain - tubulin complex
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