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1H, 13C and 15N resonance assignments of the complement control protein modules of the complement component C7 |
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| Authors: | Carla Clark Chuong-Thu Thai Marie M Phelan Juraj Bella Du?an Uhrín Ronald T Ogata Paul N Barlow Janice Bramham |
| Institution: | 1. Edinburgh Biomolecular NMR Unit, Joseph Black Building, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, Scotland, UK 2. Torrey Pines Institute for Molecular Studies, 3550 General Atomics Court, San Diego, CA, USA 3. Centre for Translational and Chemical Biology, Michael Swann Building, University of Edinburgh, Mayfield Road, Edinburgh, EH9 3JR, Scotland, UK |
| 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 (1H, 13C and 15N) assignments, respectively, have been completed. The chemical shifts and assignments have been deposited in the BioMagResBank database under accession number 18530. |
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