A cluster of positively charged amino acids in the α-chain of C4b-binding protein (C4BP) is pivotal for the regulation of the complement system and the interaction with bacteria

Scandinavian Journal of Clinical and Laboratory Investigation, Supplement

Volumn 60, Issue 233, 2000, Pages 37-49

  Blom, A M ^a  

^a LUND UNIVERSITY   (Sweden)

Author keywords

C4b; C4b binding protein; Complement; M proteins; Mutagenesis; Streptococcus pyogenes

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C4B; FIBRINOGEN; HEPARIN; AMINO ACID; BACTERIAL ANTIGEN; CARRIER PROTEIN; COMPLEMENT; COMPLEMENT INHIBITOR; COMPLEMENT RECEPTOR; GLYCOPROTEIN; OUTER MEMBRANE PROTEIN; STREPTOCOCCAL M PROTEIN;

ARTICLE; BINDING SITE; COMPLEMENT SYSTEM; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; STREPTOCOCCUS PYOGENES; BACTERIUM; CHEMICAL STRUCTURE; CHEMISTRY; COMPLEMENT ACTIVATION; ELECTROCHEMISTRY; GENETICS; HUMAN; IMMUNOLOGY; IN VITRO STUDY; METABOLISM; MUTATION;

AMINO ACIDS; ANTIGENS, BACTERIAL; BACTERIA; BACTERIAL OUTER MEMBRANE PROTEINS; BINDING SITES; CARRIER PROTEINS; COMPLEMENT ACTIVATION; COMPLEMENT C3-C5 CONVERTASES; COMPLEMENT C4B; COMPLEMENT INACTIVATOR PROTEINS; COMPLEMENT SYSTEM PROTEINS; ELECTROCHEMISTRY; GLYCOPROTEINS; HUMANS; MODELS, MOLECULAR; MUTATION; RECEPTORS, COMPLEMENT;

EID: 0034351825     PISSN: 0085591X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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