1H, 13C and 15N resonance assignments of the complement control protein modules of the complement component C7

Autor: Chuong-Thu Thai, Carla Clark, Dušan Uhrín, Ronald T. Ogata, Paul N. Barlow, Juraj Bella, Marie M. Phelan, Janice Bramham
Rok vydání: 2012
Předmět:
Zdroj: Biomolecular NMR Assignments. 7:285-288
ISSN: 1874-270X
1874-2718
DOI: 10.1007/s12104-012-9429-3
Popis: 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.
Databáze: OpenAIRE
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