Structural transitions of complement component C3 and its activation products
N Nishida, T Walz, TA Springer - Proceedings of the …, 2006 - National Acad Sciences
N Nishida, T Walz, TA Springer
Proceedings of the National Academy of Sciences, 2006•National Acad SciencesComplement 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≈ 100
Å, 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 …
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≈ 100
Å, 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 …
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 ≈100 Å, 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.
National Acad Sciences