Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein
| Autor: | Nina Luckgei, François Penin, Jean-Baptiste Marchand, Beat H. Meier, Fergal Hill, Birgit Habenstein, Anja Böckmann, Simon Megy, Francesco Ravotti |
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| Předmět: |
Coiled coil
Stereochemistry C4b-binding protein Chemistry Binding protein Complement C4b-Binding Protein Molecular Sequence Data Biochemistry C4-binding protein Oligomerization domain Solid-state NMR Assignments Secondary structure Protein Structure Secondary 3. Good health Complement system Protein Structure Tertiary Crystallography Solid-state nuclear magnetic resonance Structural Biology Humans Amino Acid Sequence Protein Multimerization Protein secondary structure Peptide sequence Nuclear Magnetic Resonance Biomolecular |
| Zdroj: | Biomolecular NMR assignments BIOMOLECULAR NMR ASSIGNMENTS Biomolecular NMR Assignments, 8 (1) |
| ISSN: | 1874-270X |
| DOI: | 10.1007/s12104-012-9440-8 |
| Popis: | 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. ISSN:1874-270X ISSN:1874-2718 |
| Databáze: | OpenAIRE |
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