EC Number   |
Subunits |
Reference |
|---|
   3.4.21.41 | homodimer |
2 * 90000, component C1r, calculated from amino acid sequence |
755267 |
| 3.4.21.41 | More |
C1 complex structure |
683195 |
| 3.4.21.41 | More |
C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex |
732102 |
| 3.4.21.41 | More |
C1rbar and the proenzyme C1r are noncovalent dimers, the subunit of C1r has a MW of 53000-85000 Da, SDS-PAGE |
81403 |
| 3.4.21.41 | More |
each C1r monomer consists of six domains, CUB1-EGF-CUB2-CCP1-CCP2-SP, i.e. an N-terminal CUB module, an EGF-like module, a second CUB module, two complement control modules CCP, and a serine protease domain SP. The three domains that constitute the catalytic fragment of C1r (CCP1-CCP2-SP) readily form head-to-tail dimers. The CUB1-EGF-CUB2 fragments of C1r also dimerize |
732889 |
| 3.4.21.41 | More |
on activation the single polypeptide chain of C1r is cleaved probably at a single position, the C1rbar subunits consist of 1 polypeptide chain of 56000 Da, A-chain, that is disulfide-linked to a 27000 Da B-chain |
81395 |
| 3.4.21.41 | More |
the C1 complex comprises two loosely interacting subunits, C1q and the Ca2+-dependent C1s-C1r-C1r-C1s tetramer. Binding of C1 to activator is mediated by C1q and triggers activation of proenzyme C1r into an active protease C1rbar, which in turn activates C1s, thereby initiating the classical pathway of complement |
81390 |
