Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein
Luckgei, Nina ; Habenstein, Birgit ; Ravotti, Francesco ; Megy, Simon ; Penin, Francois ; Marchand, Jean-Baptiste ; Hill, Fergal ; Böckmann, Anja ; Meier, Beat
In: Biomolecular NMR Assignments, 2014, vol. 8, no. 1, p. 1-6
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- 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.