How Novel Structures Inform Understanding of Complement Function

Semin Immunopathol. 2018 Jan;40(1):3-14. doi: 10.1007/s00281-017-0643-z. Epub 2017 Aug 14.

Abstract

During the last decade, the complement field has experienced outstanding advancements in the mechanistic understanding of how complement activators are recognized, what C3 activation means, how protein complexes like the C3 convertases and the membrane attack complex are assembled, and how positive and negative complement regulators perform their function. All of this has been made possible mostly because of the contributions of structural biology to the study of the complement components. The wealth of novel structural data has frequently provided support to previously held knowledge, but often has added alternative and unexpected insights into complement function. Here, we will review some of these findings focusing in the alternative and terminal complement pathways.

Keywords: C3\C5 convertase; Complement; Complement regulators; Factor H; Membrane attack complex; Structural biology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Carrier Proteins
  • Complement Activation / immunology
  • Complement C3-C5 Convertases / chemistry
  • Complement C3-C5 Convertases / immunology
  • Complement C3-C5 Convertases / metabolism
  • Complement System Proteins / chemistry*
  • Complement System Proteins / physiology*
  • Host-Pathogen Interactions / immunology
  • Humans
  • Protein Binding
  • Protein Conformation
  • Signal Transduction
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Carrier Proteins
  • Complement System Proteins
  • Complement C3-C5 Convertases