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The serine protease domains of C1r and C1s 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.
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Periodontal Ehlers-Danlos Syndrome in at least the great majority of cases results from specific classes of heterozygous mutations in C1R and C1S.
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C1q exists as the C1 complex (C1qC1r2C1s2), and C1q binding to ligands activates the C1r/C1s proteases. Incubation of nucleoli with C1 caused degradation of the nucleolar proteins nucleolin and nucleophosmin 1. T
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TNT003, an inhibitor of the serine protease C1s, prevents complement activation induced by cold agglutinins.
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Data indicate that complement C1s mRNA level was low in ICR-derived glomerulonephritis (ICGN) mice liver as compared with age-matched ICR mice.
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Analysis of its interaction properties by surface plasmon resonance shows that rC1q retains the ability of serum C1q to associate with the C1s-C1r-C1r-C1s tetramer, to recognize physiological C1q ligands such as IgG and pentraxin 3
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A molecular switch governs the interaction between the human complement protease C1s and its substrate, complement C4.
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Four positively charged amino acids on the serine protease domain appear to form a catalytic exosite that is required for efficient cleavage of C4 in the classical pathway of complement.
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These results provide further structural insights into the architecture of the C1 complex, and the interactions between C1r and C1s.
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Detailed mapping of post-translational modifications and insights into the C1r/C1s binding sites.
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Interaction with the prime side residues at the cleavage point in C1s enhances the affinity of the enzyme for complement 2 and complement 4 substrates; these prime subsite residues mediate positive cooperativity in the cleavage of the substrate.
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full specificity of the enzyme using a randomized phage display library
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There are splice variants of C1s mRNA transcripts in normal human cells
