Formation of Salt Bridges Mediates Internal Dimerization of Myosin VI Medial Tail Domain
نویسندگان
چکیده
منابع مشابه
Formation of salt bridges mediates internal dimerization of myosin VI medial tail domain.
The unconventional motor protein, myosin VI, is known to dimerize upon cargo binding to its C-terminal end. It has been shown that one of its tail domains, called the medial tail domain, is a dimerization region. The domain contains an unusual pattern of alternating charged residues and a few hydrophobic residues. To reveal the unknown dimerization mechanism of the medial tail domain, we employ...
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Although myosin VI has properties that would allow it to function optimally as a dimer, full-length myosin VI exists as a monomer in isolation. Based on the ability of myosin VI monomers to dimerize when held in close proximity, we postulated that cargo binding normally regulates dimerization of myosin VI. We tested this hypothesis by expressing a known dimeric cargo adaptor protein of myosin V...
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absorbed in the atmosphere, the NIR water vapor bands. Thus, we see no way of defending Stephen's statement that conclusions based on broad-band measurements (1) are inconsistent with other existing data sets where discrepancies were found to occur between measurements in spectral bands and theory. Instead, the broad-band solar absorption findings presented in our report (1) are entirely consis...
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absorbed in the atmosphere, the NIR water vapor bands. Thus, we see no way of defending Stephen's statement that conclusions based on broad-band measurements (1) are inconsistent with other existing data sets where discrepancies were found to occur between measurements in spectral bands and theory. Instead, the broad-band solar absorption findings presented in our report (1) are entirely consis...
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ژورنال
عنوان ژورنال: Structure
سال: 2010
ISSN: 0969-2126
DOI: 10.1016/j.str.2010.09.011