EC Number   |
|---|
   3.4.21.B7 | catalytic region of MASP-1, hanging-drop vapour-diffusion method, the best crystal diffract to 2.55 A resolution and belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.4, b = 70.4, c = 121.4 A |
| 3.4.21.B7 | hanging drop vapor diffusion method, X-ray structure of the CUB1-EGF-CUB2 domain of human MASP-1/3, responsible for interaction of MASP-1 and -3 with their partner proteins mannan-binding lectin and ficolins, is solved to a resolution of 2.3 A |
| 3.4.21.B7 | in complex with Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN, to 1.28 A resolution. Structure reveals significant plasticity of the protease |
| 3.4.21.B7 | MASP-1 catalytic domain in complex with protease inhibitor SGPI-1, recombinant CCP1-CCP2-SP fragment of MASP-1 and SGMI-1 inhibitor are mixed in a 2:3 molar ratio and concentrated to 5 mg/ml, hanging drop vapor diffusion method, mixing of 0.001 ml of protein and 0.001 ml of reservoir solution comprising 0.1 M HEPES, pH 7.0, 25% PEG 1000, 0.3 M NaNO3, at 20°C, crystal structure determination and analysis at 3.2 A resolution, molecular replacement |
| 3.4.21.B7 | 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-1 and its substrate MASP-2 are flexible at multiple sites and this flexibility may permit both intra- and inter-complex activation |
| 3.4.21.B7 | the collagen-like domain of mannan-binding lectin in complex with the binding domain of its associated protease MASP-1 |
