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Lookup NU author(s): Professor David KavanaghORCiD
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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.
Author(s): Morgan HP, Schmidt CO, Guariento M, Blaum BS, Gillespie D, Herbert AP, Kavanagh D, Mertens HD, Svergun DI, Johansson CM, Uhrin D, Barlow PN, Hannan JP
Publication type: Article
Publication status: Published
Journal: Nature Structural and Molecular Biology
Year: 2011
Volume: 18
Issue: 4
Pages: 463-470
Print publication date: 13/02/2011
ISSN (print): 1545-9993
ISSN (electronic): 1545-9985
Publisher: Nature Publishing Group
URL: http://dx.doi.org/10.1038/nsmb.2018
DOI: 10.1038/nsmb.2018
PubMed id: 21317894
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