CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.10 | Ribbon |
|
2.10.70 | Complement Module; domain 1 |
|
2.10.70.10 | Complement Module, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Complement Module, domain 1 |
| Functional Family | Mannan-binding lectin serine protease 1 |
Enzyme Information
| 3.4.21.104 |
Mannan-binding lectin-associated serine protease-2.
based on mapping to UniProt O00187
Selective cleavage after Arg-223 in complement component C2 (-Ser- Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).
-!- Mannan-binding lectin (MBL) recognizes patterns of neutral carbohydrates, such as mannose and N-acetylglucosamine, on a wide range of microbial surfaces and is able to initiate activation of the lectin pathway of complement. -!- Displays C1s-like esterolytic activity (cf. EC 3.4.21.42). -!- It also cleaves C4 and C2 with efficiencies that are relatively higher than those of EC 3.4.21.42. -!- Belongs to peptidase family S1A.
|
UniProtKB Entries (1)
| O00187 |
MASP2_HUMAN
Homo sapiens
Mannan-binding lectin serine protease 2
|
PDB Structure
| PDB | 1Q3X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions
J.Mol.Biol.
|
