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The serine protease (Montrer F2 Protéines) domains of C1r and C1s (Montrer C1S Protéines) are at the periphery of the C1r2s2 tetramer both when alone or within the nonactivated C1 complex. The C1 complex adopts a conformation incompatible with intramolecular activation of C1. Instead, intermolecular proteolytic activation between neighboring C1 complexes bound to a complement-activating surface occurs. Many structurally unrelated molecular patterns can activate C1.
We identified a novel, homozygous, loss-of-function mutation (p.Pro445Leufs*11) in the C1R gene. Using the Sanger method of DNA sequencing in 14 family members, we confirmed the presence of the mutation in 4 patients with early-onset systemic lupus erythematosus and in an asymptomatic 9-year-old girl. Complement levels were low in sera from patients with truncated C1r protein.
Periodontal Ehlers-Danlos Syndrome in at least the great majority of cases results from specific classes of heterozygous mutations in C1R and C1S (Montrer C1S Protéines).
We confirmed increased levels of C1R and VTN (Montrer VTN Protéines) in sera from patients with Joint hypermobility syndrome by western blot analyses
C1q exists as the C1 complex (C1qC1r2C1s2), and C1q binding to ligands activates the C1r/C1s (Montrer C1S Protéines) proteases. Incubation of nucleoli with C1 caused degradation of the nucleolar proteins nucleolin (Montrer NCL Protéines) and nucleophosmin 1 (Montrer NPM1 Protéines). T
C1r specificity is well suited to its cleavage targets and that efficient cleavage of C1s (Montrer C1S Protéines) is achieved through both active site and exosite contributions.
Analysis of its interaction properties by surface plasmon resonance shows that rC1q retains the ability of serum C1q to associate with the C1s (Montrer C1S Protéines)-C1r-C1r-C1s (Montrer C1S Protéines) tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3 (Montrer PTX3 Protéines)
a structural rearrangement as a switch between functional states of human C1r
These results provide further structural insights into the architecture of the C1 complex, and the interactions between C1r and C1s (Montrer C1S Protéines).
The modular C1r protein is the first protease activated in the classical complement pathway, a key component of innate immunity.
C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.
complement C1r subcomponent
, complement C1r
, complement component 1, r subcomponent
, complement component 1 subcomponent r