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

Biomol NMR Assign. 2009 Jun;3(1):49-52. doi: 10.1007/s12104-008-9139-z. Epub 2009 Jan 13.

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 (1)H, (15)N and (13)C 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carbon Isotopes / chemistry
  • Complement C7 / chemistry*
  • Complement C7 / ultrastructure*
  • Fibrinogen / chemistry*
  • Fibrinogen / ultrastructure*
  • Magnetic Resonance Spectroscopy / methods*
  • Molecular Sequence Data
  • Nitrogen Isotopes / chemistry
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protons

Substances

  • Carbon Isotopes
  • Complement C7
  • Nitrogen Isotopes
  • Protons
  • Fibrinogen