3j1u

Low affinity dynein microtubule binding domain - tubulin complex

spinqualitylabelsall models 3j1u, resolution 9.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3j1u is a 3 chain structure with sequence from Bos taurus and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3j1t Gene: Dync1h1, Dhc1, Dnch1, Dnchc1, Dyhc (LK3 transgenic mice) Resources: FirstGlance, OCA, RCSB, PDBsum Disease [DYHC1_MOUSE] Defects in Dync1h1 are the cause of the 'Legs at odd angles' (LOA) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth. LOA mutants display defects in migration of facial motor neuron cell bodies and impaired retrograde transport in spinal cord motor neurons. Defects in Dync1h1 are the cause of the Cramping 1 (Cra1) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth. Function [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. 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dynein Tubulin

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