Positively charged amino acids at the interface between α-chain CCP1 and CCP2 of C4BP are required for regulation of the classical C3-convertase

Author:

Blom Anna M.,Zadura Anna Foltyn,Villoutreix Bruno O.,Dahlbäck Björn

Publisher

Elsevier BV

Subject

Molecular Biology,Immunology

Reference42 articles.

1. Binding of human complement component C4b-binding protein (C4BP) to Streptococcus pyogenes involves the C4b-binding site;Accardo;J. Immunol.,1996

2. Inhibition of complement components C3 and C4 by cadralazine and its active metabolite;Andersson;Eur. J. Clin. Pharmacol.,1991

3. Solution structure of a pair of complement modules by nuclear magnetic resonance;Barlow;J. Mol. Biol.,1993

4. Bordetella pertussis binds the human complement regulator C4BP: role of filamentous hemagglutinin;Berggård;Infect. Immun.,1997

5. A cluster of positively charged amino acids in the N-terminal modules of the C4BP α-chain is crucial for C4b binding and factor I cofactor function;Blom;J. Biol. Chem.,1999

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