Topological mapping of complement component C9 by recombinant DNA techniques suggests a novel mechanism for its insertion into target membranes.

摘要: cDNA molecules coding for mouse and trout C9 have been isolated the derived amino acid sequences compared with that of human C9. Regions high homology between closely related species (mouse human) correlate putative domains in protein structure supporting a model having five globular domains. Comparison more distant (trout suggests regions particular importance to function. In addition three allow secondary be predicted confidence we tested prediction by mapping surface features protein. Reported here is recombinant DNA approach fine antibody epitopes. Two are connected stretch about 40 residues which characteristic individual conformational forms concentrated. We suggest this region might act as hinge allowing rearrangement necessary membrane insertion. inserting domain one highly conserved sequence has potential form an amphipathic alpha-helix once it buried lipid bilayer. These novel mechanism irreversible, post-translational insertion into target membranes.