Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein.
Biomol NMR Assign
; 8(1): 1-6, 2014 Apr.
Article
in En
| MEDLINE
| ID: mdl-23138856
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Nuclear Magnetic Resonance, Biomolecular
/
Complement C4b-Binding Protein
/
Protein Multimerization
Limits:
Humans
Language:
En
Journal:
Biomol NMR Assign
Journal subject:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Year:
2014
Document type:
Article
Affiliation country:
France