Structural and functional aspects of C1-inhibitor

Immunobiology. 2002 Sep;205(4-5):518-33. doi: 10.1078/0171-2985-00151.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blood Coagulation / physiology
  • Complement C1 Inactivator Proteins / chemistry*
  • Complement C1 Inactivator Proteins / genetics
  • Complement C1 Inactivator Proteins / metabolism*
  • Complement C1 Inhibitor Protein
  • Complement Pathway, Classical / physiology
  • Humans
  • Image Processing, Computer-Assisted*
  • Molecular Sequence Data
  • Mutation
  • Protein Structure, Secondary*
  • Recombinant Proteins
  • Sequence Homology, Amino Acid

Substances

  • Complement C1 Inactivator Proteins
  • Complement C1 Inhibitor Protein
  • Recombinant Proteins