Ultrastructure of human C4-binding protein: proposition for a new model.
The structure of human C4-binding protein (C4bp), a regulatory factor of the classical C3 convertase of complement, has been under investigation for several years, but remains poorly understood. For example, the number of subunits in the C4bp molecule has not been established. In this report, we use two different techniques (partial reduction and electron microscopy) to clarify the structure of the C4bp. Our results lead us to propose a structural model which is quite different to that suggested before, i.e. the C4bp molecule appears to be a decamer. In addition to the disulfide bonds which link each subunit to another, a second disulfide interaction leads to the association of the subunits in pairs. Each pair of subunits appears as a filament ending in a globular head at the N-terminal extremity. The pairs of subunits join to form a conical central domain (at the C-terminal extremity) linked by disulfide bonds. The proposed pentameric shape of the C4bp is consistent with the stoichiometry of the C4b-C4bp interactions. The proposed model indicates an overall structural homology between C4bp and other binding proteins.
D002352:Carrier Proteins / Q000302:isolation & purification*; D003181:Complement C4; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D016167:Integrin alphaXbeta2; D008854:Microscopy, Electron; D008954:Models, Biological; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate
D002352:Carrier Proteins; D003181:Complement C4; D016167:Integrin alphaXbeta2; D012967:Sodium Dodecyl Sulfate