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

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Original languageEnglish
Pages (from-to)285-288
Number of pages4
JournalBiomolecular NMR Assignments
Volume7
Issue number2
Early online date17 Sep 2012
DOIs
Publication statusPublished - Oct 2013

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 (H-1, C-13 and N-15) assignments, respectively, have been completed. The chemical shifts and assignments have been deposited in the BioMagResBank database under accession number 18530.

    Research areas

  • Complement, Membrane attack complex, Pore-forming, CCPs, NMR, Resonance assignment, FACTOR-I MODULES, C6, IDENTIFICATION, DOMAIN, C345C

ID: 5131130