¹H, ¹³C and ¹⁵N resonance assignments of the complement control protein modules of the complement component C7.
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 ((1)H, (13)C and (15)N) assignments, respectively, have been completed. The chemical shifts and assignments have been deposited in the BioMagResBank database under accession number 18530.
Edinburgh Biomolecular NMR Unit, Joseph Black Building, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, Scotland, UK.
Carla
C
Clark
Chuong-Thu
CT
Thai
Marie M
MM
Phelan
Juraj
J
Bella
Dušan
D
Uhrín
Ronald T
RT
Ogata
Paul N
PN
Barlow
Janice
J
Bramham
D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D003184:Complement C7 / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011522:Protons; D016415:Sequence Alignment
D002247:Carbon Isotopes; D003184:Complement C7; D009587:Nitrogen Isotopes; D011522:Protons