{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Redwine WB"],"funding":["NIH HHS"],"pagination":["1532-1536"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3919166"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["337(6101)"],"pubmed_abstract":["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."],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Structural basis for microtubule binding and release by dynein."],"pmcid":["PMC3919166"],"funding_grant_id":["DP2 OD004268","1 DP2 OD004268-1"],"pubmed_authors":["Hernandez-Lopez R","Huang J","Leschziner AE","Reck-Peterson SL","Redwine WB","Zou S"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis for microtubule binding and release by dynein.","description":"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.","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Sep","modification":"2024-11-20T22:08:59.931Z","creation":"2019-03-27T01:21:39Z"},"accession":"S-EPMC3919166","cross_references":{"pubmed":["22997337"],"doi":["10.1126/science.1224151"]}}