Structural and functional aspects of C1-inhibitor.
C1-Inh is a serpin that inhibits serine proteases from the complement and the coagulation pathway. C1-Inh consists of a serpin domain and a unique N-terminal domain and is heavily glycosylated. Non-functional mutants of C1-Inh can give insight into the inhibitory mechanism of C1-Inh. This review describes a novel 3D model of C1-Inh, based on a newly developed homology modelling method. This model gives insight into a possible potentiation mechanism of C1-Inh and based on this model the essential residues for efficient inhibition by C1-Inh are discussed.
Bos
Ineke G A
IG
Dept. Immunopathology, Academical Medical Centre, University of Amsterdam, The Netherlands. I_Bos@clb.nl
Hack
C Erik
CE
Abrahams
Jan Pieter
JP
D000595:Amino Acid Sequence; D000818:Animals; D001777:Blood Coagulation / Q000502:physiology; D003174:Complement C1 Inactivator Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D050718:Complement C1 Inhibitor Protein; D003171:Complement Pathway, Classical / Q000502:physiology; D006801:Humans; D007091:Image Processing, Computer-Assisted; D008969:Molecular Sequence Data; D009154:Mutation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins; D017386:Sequence Homology, Amino Acid
D003174:Complement C1 Inactivator Proteins; D050718:Complement C1 Inhibitor Protein; D011994:Recombinant Proteins