Ontology highlight
ABSTRACT:
SUBMITTER: Morgan HP
PROVIDER: S-EPMC3512577 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Morgan Hugh P HP Schmidt Christoph Q CQ Guariento Mara M Blaum Bärbel S BS Gillespie Dominic D Herbert Andrew P AP Kavanagh David D Mertens Haydyn D T HD Svergun Dmitri I DI Johansson Conny M CM Uhrín Dušan D Barlow Paul N PN Hannan Jonathan P JP
Nature structural & molecular biology 20110213 4
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 mer ...[more]