4.0 Article

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

Journal

BIOMOLECULAR NMR ASSIGNMENTS
Volume 3, Issue 1, Pages 49-52

Publisher

SPRINGER
DOI: 10.1007/s12104-008-9139-z

Keywords

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

Funding

  1. Medical Research Council of the U. K. [G0500940]
  2. The Wellcome Trust
  3. National Institute of Health [GM29831]
  4. MRC [G0500940] Funding Source: UKRI
  5. Medical Research Council [G0500940] Funding Source: researchfish

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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 H-1, N-15 and C-13 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.

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