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4byf

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Revision as of 09:24, 26 March 2014 by OCA (Talk | contribs)
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Template:STRUCTURE 4byf

Contents

Crystal structure of human Myosin 1c in complex with calmodulin in the pre-power stroke state

Template:ABSTRACT PUBMED 24636949

Function

[MYO1C_HUMAN] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes (By similarity). Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation (By similarity).

About this Structure

4byf is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  • Stefan Munnich MH, Manstein DJ. Crystal Structure of Human Myosin 1c - The Motor in GLUT4 Exocytosis: Implications for Ca-Regulation and 14-3-3 Binding. J Mol Biol. 2014 Mar 14. pii: S0022-2836(14)00128-4. doi:, 10.1016/j.jmb.2014.03.004. PMID:24636949 doi:http://dx.doi.org/10.1016/j.jmb.2014.03.004

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