期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 18, 期 4, 页码 463-U101出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2018
关键词
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资金
- Wellcome Trust
- Scottish University Life Sciences Alliance
- UK Biotechnology and Biological Sciences Research Council
- Wellcome Trust [081179, 078780/Z/05/Z]
- EastChem PhD studentship
- University of Edinburgh
- EC [MEST-CT-2005-020744]
- MRC [G0001089] Funding Source: UKRI
- Wellcome Trust [078780/Z/05/Z] Funding Source: Wellcome Trust
- Medical Research Council [G0001089] Funding Source: researchfish
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.
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