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EC Number
x * 88000, C1r zymogen, domain structure, overview
2 * 83000, SDS-PAGE of reduced protein, gel filtration in 6 M guanidinium hydrochloride
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
CCP1 is essential to the assembly of the dimer, but formation of a stable dimer is not a prerequisite for self-activation
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
C1q, 2 * C1s, 2 * C1r
C1 complex structure
C1r and C1s pro-enzymes form a heterotetrameric structure that associates with the recognition molecule, C1q, in the C1 complex
C1rbar and the proenzyme C1r are noncovalent dimers, the subunit of C1r has a MW of 53000-85000 Da, SDS-PAGE
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
Results 1 - 10 of 12 > >>