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Structural basis for engagement by complement factor H of C3b on a self surface.

Morgan H.P., Schmidt C.Q., Guariento M., Blaum B.S., Gillespie D., Herbert A.P., Kavanagh D., Mertens H.D., Svergun D.I., Johansson C.M., Uhrin D., Barlow P.N., Hannan J.P.

Complement factor H (FH) attenuates C3b molecules tethered by their thioester domains to self surfaces and thereby protects host tissues. Factor H is a cofactor for initial C3b proteolysis that ultimately yields a surface-attached fragment (C3d) corresponding to the thioester domain. We used NMR and X-ray crystallography to study the C3d-FH19-20 complex in atomic detail and identify glycosaminoglycan-binding residues in factor H module 20 of the C3d-FH19-20 complex. Mutagenesis justified the merging of the C3d-FH19-20 structure with an existing C3b-FH1-4 crystal structure. We concatenated the merged structure with the available FH6-8 crystal structure and new SAXS-derived FH1-4, FH8-15 and FH15-19 envelopes. The combined data are consistent with a bent-back factor H molecule that binds through its termini to two sites on one C3b molecule and simultaneously to adjacent polyanionic host-surface markers.

Nat. Struct. Mol. Biol. 18:463-470(2011) [PubMed] [Europe PMC]

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