EC Number   |
|---|
   3.4.21.104 | - |
| 3.4.21.104 | C-terminal catalytic region of MASP-2, X-ray diffraction structure determination and anaylsis |
| 3.4.21.104 | catalytic fragment encompassing the second complement control protein module and the serine protease domain, in presence of Na+, in absence of Mg2+, 0.8 mg/ml purified recombinant protein in 140 mM NaCl, 20 mM Tris-HCl, pH 7.4, and 0.05% w/v NaN3, hanging drop vapour diffusion method at 20°C, mixing with equal volume of reservoir solution containing 30% w/v PEG 6000, 0.2 M NaCl, 10% v/v glycerol, 0.1 M Tris-HCl, pH 7.5, X-ray diffraction structure determination and analysis at 2.25 A resolution |
| 3.4.21.104 | hanging drop vapor diffusion method in the presence of Ca2+ |
| 3.4.21.104 | in complex with Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN, to 1.28 A resolution. Strucutre reveals significant plasticity of the protease |
| 3.4.21.104 | structures of Ca2+-bound MASP dimers. Solution structures of the CUB1-EGF-CUB2 dimer indicate that the two CUB2 domains are tilted by 90 degreees compared with the crystal structures. Solution structures of the full-length MASP dimers in their zymogen and activated forms reveal similar structures that are much more bent than anticipated. MASP-2 and its activator MASP-1 are flexible at multiple sites and this flexibility may permit both intra- and inter-complex activation |
| 3.4.21.104 | zymogen and the activated form, 2.4 A resolution |
