H-1, C-13 and N-15 resonance assignments of the complement control protein modules of the complement component C7

Carla Clark, [No Value] Chuong-Thu Thai, Marie M. Phelan, Juraj Bella, Dusan Uhrin, Ronald T. Ogata, Paul N. Barlow, Janice Bramham*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Human C7 is one of four homologous complement proteins that self-assemble on the nascent activation-specific fragment, C5b, thus forming the cytolytic membrane attack complex (MAC). In addition to the conserved modular core of the MAC/perforin protein family, C7 has four C-terminal domains comprising a pair of complement control protein modules (CCPs) preceding two Factor-I like modules (FIMs). It is proposed that the C7-CCPs might serve as a molecular arm for delivery of C7-FIMs to their binding site on C5b. Here we present the NMR chemical shift assignments for the C7-CCPs produced as a 14-kDa recombinant protein. Based upon triple-resonance experiments, 98 and 94 % of the backbone and side-chain (H-1, C-13 and N-15) assignments, respectively, have been completed. The chemical shifts and assignments have been deposited in the BioMagResBank database under accession number 18530.

Original languageEnglish
Pages (from-to)285-288
Number of pages4
JournalBiomolecular NMR Assignments
Volume7
Issue number2
Early online date17 Sep 2012
DOIs
Publication statusPublished - Oct 2013

Keywords

  • Complement
  • Membrane attack complex
  • Pore-forming
  • CCPs
  • NMR
  • Resonance assignment
  • FACTOR-I MODULES
  • C6
  • IDENTIFICATION
  • DOMAIN
  • C345C

Fingerprint

Dive into the research topics of 'H-1, C-13 and N-15 resonance assignments of the complement control protein modules of the complement component C7'. Together they form a unique fingerprint.

Cite this