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. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000082700Publication status
publishedExternal links
Journal / series
Biomolecular NMR AssignmentsVolume
Pages / Article No.
Publisher
SpringerSubject
C4-binding protein; Oligomerization domain; Solid-state NMR; Assignments; Secondary structureOrganisational unit
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
Notes
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher.More
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