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- Title
Structural basis for engagement by complement factor H of C3b on a self surface.
- Authors
Morgan, Hugh P; Schmidt, Christoph Q; Guariento, Mara; Blaum, Bärbel S; Gillespie, Dominic; Herbert, Andrew P; Kavanagh, David; Mertens, Haydyn D T; Svergun, Dmitri I; Johansson, Conny M; Uhrín, Dušan; Barlow, Paul N; Hannan, Jonathan P
- Abstract
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.
- Publication
Nature structural & molecular biology, 2011, Vol 18, Issue 4, p463
- ISSN
1545-9985
- Publication type
Journal Article
- DOI
10.1038/nsmb.2018