The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
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چکیده
منابع مشابه
The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
HAMP domains connect extracellular sensory with intracellular signaling domains in over 7500 proteins, including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. The solution structure of an archaeal HAMP domain shows a homodimeric, four-helical, parallel coiled coil with unusual interhelical packing, related to the canonical packing by rotation of the helices. This...
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UNLABELLED HAMP domains are α-helical coiled coils that often transduce signals from extracytoplasmic sensing domains to cytoplasmic domains. Limited structural information has resulted in hypotheses that specific HAMP helix movement changes downstream enzymatic activity. These hypotheses were tested by mutagenesis and cysteine cross-linking analysis of the PhoQ histidine kinase, essential for ...
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ژورنال
عنوان ژورنال: Cell
سال: 2006
ISSN: 0092-8674
DOI: 10.1016/j.cell.2006.06.058