EC Number   |
Subunits |
Reference |
|---|
   3.4.21.41 | dimer |
2 * 83000, SDS-PAGE of reduced protein, gel filtration in 6 M guanidinium hydrochloride |
81393 |
| 3.4.21.41 | dimer |
2 * 85000, the C1rbar subunits consist of one polypeptide chain of 56000 Da, A-chain, that is disulfide-linked to a 27000 Da B-chain, SDS-PAGE |
81395 |
| 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 | heteropentamer |
C1q, 2 * C1s, 2 * C1r |
717805 |
| 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 | dimer |
CCP1 is essential to the assembly of the dimer, but formation of a stable dimer is not a prerequisite for self-activation |
652176 |
| 3.4.21.41 | dimer |
deletion of CCP1 domain from CCP1-CCP2-SP fragment results in the loss of the dimeric structure. Dimerization of C1r is not a prerequisite for autoactivation |
652680 |
| 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 |
