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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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    Titel
    • Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein
    Autor
    • Luckgei, Nina. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Habenstein, Birgit. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Ravotti, Francesco. Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    • Megy, Simon. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Penin, Francois. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Marchand, Jean-Baptiste. IMAXIO SA, 181-203 avenue Jean Jaurès, 69007, Lyon, France
    • Hill, Fergal. IMAXIO SA, 181-203 avenue Jean Jaurès, 69007, Lyon, France
    • Böckmann, Anja. Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS, Université de Lyon 1, 7 passage du Vercors, 69367, Lyon, France
    • Meier, Beat. Physical Chemistry, ETH Zurich, Wolfgang-Pauli-Strasse 10, 8093, Zurich, Switzerland
    Dokumententyp
    • Postprint
    Sprache
    • Englisch
    Veröffentlicht in
    • Biomolecular NMR Assignments, 2014, vol. 8, no. 1, p. 1-6. Springer Netherlands
    Andere elektronische Ausgabe
    OAI-PMH-ID
    • oai:doc.rero.ch:325226
    Summary
    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.