ArticleThe EMBO journal2011
Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
What it found
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Who cites it
46 citing papers in PubMed, 84 citations in OpenAlex.
- The resistance to Toxoplasma gondii in Microtus fortis is associated with the activation of the complement lectin pathway.PLoS neglected tropical diseases · 2026Article
- Complement C3 recognition by C3 convertases.Science advances · 2026Article
- Modulator-induced conformational changes in complement C5, implications for function and drug design.Frontiers in immunology · 2026Article
- Description and phenotype of a novel C5 gene mutation and a novel combination: family report and literature review.Frontiers in immunology · 2025Review
- The Crystal Structure of the Michaelis-Menten Complex of C1 Esterase Inhibitor and C1s Reveals Novel Insights into Complement Regulation.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- CG001, a C3b-targeted complement inhibitor, blocks 3 complement pathways: development and preclinical evaluation.Blood advances · 2024Article
- Structural Model for Factor X Inhibition of IgM and Complement-Mediated Neutralization of Adenovirus.Viruses · 2023Article
- Protein therapeutics and their lessons: Expect the unexpected when inhibiting the multi-protein cascade of the complement system.Immunological reviews · 2023Review
- Structural modelling of human complement FHR1 and two of its synthetic derivatives provides insight into their in-vivo functions.Computational and structural biotechnology journal · 2023Article
- C3-dependent effector functions of complement.Immunological reviews · 2023Review
- Zilucoplan, a macrocyclic peptide inhibitor of human complement component 5, uses a dual mode of action to prevent terminal complement pathway activation.Frontiers in immunology · 2023Article
- Complement component C3: A structural perspective and potential therapeutic implications.Seminars in immunology · 2022Review
- The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2021Review
- Nanobodies Provide Insight into the Molecular Mechanisms of the Complement Cascade and Offer New Therapeutic Strategies.Biomolecules · 2021Review
- Article
- How Structures of Complement Complexes Guide Therapeutic Design.Sub-cellular biochemistry · 2021Review
- Deregulation of Factor H by Factor H-Related Protein 1 Depends on Sialylation of Host Surfaces.Frontiers in immunology · 2021Article
- Proteomic Investigations of Two PakistaniToxins · 2020Article
- A C3-specific nanobody that blocks all three activation pathways in the human and murine complement system.The Journal of biological chemistry · 2020Article
- An inhibitor of complement C5 provides structural insights into activation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases. These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a). We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution. The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage. CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb. A general model for substrate recognition by the convertases is presented based on the C5-CVF and C3b-Bb-SCIN structures. Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.