Long single α-helical tail domains bridge the gap between structure and function of myosin VI
Long single α-helical tail domains bridge the gap between structure and function of myosin VI
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New York: Nature Publishing Group US
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Language
English
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New York: Nature Publishing Group US
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Contents
Myosin VI has challenged the lever arm hypothesis of myosin movement because of its ability to take ∼36-nm steps along actin with a canonical lever arm that seems to be too short to allow such large steps. Here we demonstrate that the large step of dimeric myosin VI is primarily made possible by a medial tail in each monomer that forms a rare singl...
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Full title
Long single α-helical tail domains bridge the gap between structure and function of myosin VI
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2441774
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2441774
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ISSN
1545-9993
E-ISSN
1545-9985
DOI
10.1038/nsmb.1429
