Literature summary for 3.4.21.41 extracted from

Beveridge, A.J.; Wallis, R.; Samani, N.J.
A molecular dynamics study of C1r and C1s dimers: implications for the structure of the C1 complex (2012), Proteins, 80, 1987-1997.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure analysis, PDB IDs 1APQ	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00736	-	-

Subunits

Subunits	Comment	Organism
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	Homo sapiens

Synonyms

Synonyms	Comment	Organism
C1r	-	Homo sapiens
C1r protease	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	complement is an important part of the immune system. It is initiated through three different pathways known as the classical, lectin, and alternative pathway. The multimolecular C1 complex of the classical pathway consists of a subcomponent, C1q, which binds to a tetramer comprising two C1r and two C1s proteases, EC 3.4.21.41 and EC 3.4.21.42, respectively	Homo sapiens
additional information	the C1s/C1r/C1r/C1s tetramer forms a complex with C1q by interacting with the stems. C1r is a homologous multidomain protease containing 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. Interaction analysis and structure-function relationship, formation of the C1 complex, molecular dynamics simulations and thermodynamics, detailed overview	Homo sapiens
physiological function	C1r is a zymogen, activation of C1 occurs when the C1q subcomponent binds to a pathogen via its globular heads resulting in autolytic activation of C1r followed, in turn, by C1r-mediated activation of C1s	Homo sapiens

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Release 2023.1 (January 2023)