期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 36, 页码 13147-13151出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0405405101
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资金
- NIAID NIH HHS [AI022021, AI048489, P01 AI056013, R01 AI022021, R37 AI022021, R01 AI048489, AI056013] Funding Source: Medline
After binding to cellular receptors and proteolytic activation, the protective antigen component of anthrax toxin forms a heptameric prepore. The prepore later undergoes pH-dependent conversion to a pore, mediating translocation of the edema and lethal factors to the cytosol. We describe structures of the prepore (3.6 Angstrom) and a p repo re: receptor complex (4.3 Angstrom) that reveal the location of pore-forming loops and an unexpected interaction of the receptor with the pore-forming domain. Lower pH is required for prepore-to-pore conversion in the presence of the receptor, indicating that this interaction regulates pH-dependent pore formation. We present an example of a receptor negatively regulating pH-dependent membrane insertion.
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