(1)H, (15)N and (13)C resonance assignment of the pair of Factor-I like modules of the complement protein C7

Marie M. Phelan, Chuong-Thu Thai, Andrew P. Herbert, Juraj Bella, Dusan Uhrin, Ronald T. Ogata, Paul N. Barlow, Janice Bramham

Research output: Contribution to journalArticlepeer-review

Abstract

The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, disulphide-rich, protein encompassing this C-terminal domain. Using conventional triple resonance experiments 93% of the 1H, 15N and 13C assignment has been achieved, accounting for all assignment apart from a flexible N-terminus cloning artefact and an undefined loop. The chemical shifts have been deposited in the BioMagResBank; Accession No. 15996.
Original languageEnglish
Pages (from-to)49-52
Number of pages4
JournalBiomolecular NMR Assignments
Volume3
Issue number1
DOIs
Publication statusPublished - Jun 2009

Keywords

  • Complement
  • Membrane attack complex
  • MAC
  • C7
  • Factor I module
  • FIM
  • NMR
  • Resonance assignment

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