Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings.

ABSTRACT: Characterization of segmental flexibility is needed to understand the biological mechanisms of the very large category of functionally diverse proteins, exemplified by the regulators of complement activation, that consist of numerous compact modules or domains linked by short, potentially flexible, sequences of amino acid residues. The use of NMR-derived residual dipolar couplings (RDCs), in magnetically aligned media, to evaluate interdomain motion is established but only for two-domain proteins. We focused on the three N-terminal domains (called CCPs or SCRs) of the important complement regulator, human factor H (i.e., FH1-3). These domains cooperate to facilitate cleavage of the key complement activation-specific protein fragment, C3b, forming iC3b that no longer participates in the com

SUBMITTER: Maciejewski M 

PROVIDER: S-EPMC3215105 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature