Skip to main content
Article thumbnail
Location of Repository

Structure and influence of tick complement inhibitor on human complement component 5

By Folmer Fredslund, Nick S. Laursen, Pietro Roversi, Lasse Jenner, Cristiano L. P. Oliveira, Jan S. Pedersen, Miles A. Nunn, Susan M. Lea, Richard Discipio, Lars Sottrup-Jensen and Gregers R. Andersen


To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 Å. The core of C5 adopted a structure resembling that of C3, with the domain arrangement at the position corresponding to the C3 thioester being very well conserved. However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5. Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site. The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.\ud \u

Topics: Biology and Microbiology, Ecology and Environment
Year: 2008
DOI identifier: 10.1038/ni.1625
OAI identifier:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • (external link)
  • (external link)
  • (external link)
  • (external link)
  • Suggested articles

    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.