EC Number   |
Reference |
|---|
   3.4.21.47 | C3 convertase formed by C3b and the protease fragment Bb in complex with staphylococcal complement inhibitor, hanging drop vapor diffusion method, using 75 mM sodium/potassium tartrate, 8.0% (w/v) PEG 3350, 50 mM Bis-Tris propane, pH 6.5 |
710039 |
| 3.4.21.47 | crystal structures of the pro-convertase C3bB at 4 A resolution and its complex with factor D at 3.5 A resolution. Factor B binding to C3b forms an open activation state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor DĀs self-inhibitory loop. This concerted proteolytic mechanism, which is cofactordependent and substrate-induced, restricts complement amplification to C3b-tagged target cells |
718398 |
| 3.4.21.47 | engineered subunit Bb with Cys-resiudes at positions 435 and 428, in complex with inhibitors 6-amidino-2-naphthyl-4-guanidinobenzoate or diisopropyl phosphate |
670220 |
| 3.4.21.47 | in complex with factor H, hanging drop vapor diffusion method, using 7.0% (w/v) PEG 3350, 70 mM ammonium acetate, pH 7.1, at 18°C |
710040 |
| 3.4.21.47 | structural analysis of complement component C3b in complex with the macrophage-expressed complement receptor CRIg, domain architecture of complement component C3 and the C3b/C3c-CRIg complexes shown, structural similarities between complement components C3b and C3c indicated, comparison between complement components C3b and C3 reveals that complement component C3 stimulation is accompanied by major strucural rearrangements |
683917 |
