Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 52, Pages 19737-19742Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0609791104
Keywords
electron microscopy; proteolytic; thioester
Categories
Funding
- NIAID NIH HHS [R01 AI072765, R01 AI072765-26A1, AI72765] Funding Source: Medline
- NIGMS NIH HHS [GM62580, P01 GM062580] Funding Source: Medline
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Complement sensitizes pathogens for phagocytosis and lysis. We use electron microscopy to examine the structural transitions in the activation of the pivotal protein in the complement pathway, C3. In the cleavage product C3b, the position of the thioester domain moves approximate to 100 angstrom, which becomes covalently coupled to antigenic surfaces. In the iC3b fragment, cleavage in an intervening domain creates a long flexible linker between the thioester domain and the macroglobulin domain ring of C3. Studies on two products of nucleophile addition to C3 reveal a structural intermediate in activation, and a final product, in which the anaphylatoxin domain has undergone a remarkable movement through the macroglobulin ring.
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