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 language | English |
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Pages (from-to) | 49-52 |
Number of pages | 4 |
Journal | Biomolecular NMR Assignments |
Volume | 3 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jun 2009 |
Keywords
- Complement
- Membrane attack complex
- MAC
- C7
- Factor I module
- FIM
- NMR
- Resonance assignment