Dynamic structural changes during complement C3 activation analyzed by hydrogen/deuterium exchange mass spectrometry.

ABSTRACT: Proteolytic cleavage of component C3 to C3b is a central step in the activation of complement. Whereas C3 is largely biologically inactive, C3b is directly involved in various complement activities. While the recently described crystal structures of C3 and C3b provide a molecular basis of complement activation, they do not reflect the dynamic changes that occur in solution. In addition, the available C3b structures diverge in some important aspects. Here we have utilized hydrogen/deuterium exchange coupled with mass spectrometry (HDX-MS) to investigate relative changes in the solution-phase structures of C3 and C3b. By combining two forms of mass spectrometry we could maximize the primary sequence coverage of C3b and demonstrate the feasibility of this method for large plasma proteins. Whi

SUBMITTER: Schuster MC 

PROVIDER: S-EPMC2453784 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature