Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein

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.

Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase

“…17 The histidine brace is a strictly conserved feature across all LPMOs that have been structurally characterized, both in the solid state and in solution. 11,18,19…”

Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods

“…To obtain both, magic-angle sample spinning (MAS) is mandatory for most solid materials (Andrew et al 1958;Lowe and Norberg 1957). Most applications of solid-state NMR to proteins are presently based on the sequential assignment of the amide nitrogen and C 0 , Ca and Cb resonances as well as the remaining sidechain 15 N and 13 C nuclei (Pauli et al 2001;Schuetz et al 2010;Huber et al 2014;Luckgei et al 2014). This provides a large set of resonance frequencies of nuclei which are subsequently used to measure inter-nuclear distance restraints (Castellani et al 2002).…”