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• W2061888488 abstract "The complement 4 binding protein (C4bp) plays a crucial role in the inhibition of the complement cascade. It has an extraordinary seven-arm octopus-like structure with 7 tentacle-like identical chains, held together at their C-terminal end. The C-terminal domain does oligomerize in isolation, and is necessary and sufficient to oligomerize full-length C4bp. It is predicted to form a seven-helix coiled coil, and its multimerization properties make it a promising vaccine adjuvant, probably by enhancing the structural stability and binding affinity of the presented antigen. Here, we present the solid-state NMR resonance assignment of the human C4bp C-terminal oligomerization Domain, hC4pbOD, and the corresponding secondary chemical shifts." @default.
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• W2061888488 date "2012-11-09" @default.
• W2061888488 modified "2023-10-09" @default.
• W2061888488 title "Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein" @default.
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• W2061888488 doi "https://doi.org/10.1007/s12104-012-9440-8" @default.
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