Ontology highlight
ABSTRACT:
SUBMITTER: Nishida N
PROVIDER: S-EPMC1750921 | biostudies-literature | 2006 Dec
REPOSITORIES: biostudies-literature
Nishida Noritaka N Walz Thomas T Springer Timothy A TA
Proceedings of the National Academy of Sciences of the United States of America 20061215 52
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 approximately 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 ri ...[more]