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3.4.21.104: mannan-binding lectin-associated serine protease-2

This is an abbreviated version!
For detailed information about mannan-binding lectin-associated serine protease-2, go to the full flat file.

Word Map on EC 3.4.21.104

Reaction

Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile) =

Synonyms

CCP1-CCP2-SP, Mannan-binding lectin associated serine protease-2, mannan-binding lectin-associated serine protease, mannan-binding lectin-associated serine protease 2, mannan-binding lectin-associated serine protease-2, mannose-binding lectin-associated serine protease 2, mannose-binding lectin-associated serine protease-2, mannose-binding lectin-associated-serine protease-2, Map19, MASP, MASP-2, MASP-2A, MASP-2K, MASP2, MBL-associated serine protease, MBL-associated serine protease 2, MBL-associated serine protease-2, MBL-associated-serine protease-2, MBL-MASP, MBL/ficolin-associated serine protease, MBP-associated serine protease, MBP-associated serine protease 2, MBP-associated serine protease-2, S01.229

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.104 mannan-binding lectin-associated serine protease-2

Crystallization

Crystallization on EC 3.4.21.104 - mannan-binding lectin-associated serine protease-2

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal catalytic region of MASP-2, X-ray diffraction structure determination and anaylsis
-
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
in complex with Schistocerca gregaria protease inhibitor-2 variant VCTKLWCN, to 1.28 A resolution. Strucutre reveals significant plasticity of the protease
zymogen and the activated form, 2.4 A resolution
hanging drop vapor diffusion method in the presence of Ca2+
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