ArticleThe Journal of biological chemistry2016
Solution Structures of Complement C2 and Its C4 Complexes Propose Pathway-specific Mechanisms for Control and Activation of the Complement Proconvertases.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.
- Pitfalls in complement analysis: A systematic literature review of assessing complement activation.Frontiers in immunology · 2022Pooled it
- Complement Dysregulation in Kidney Diseases: Mechanisms, Biomarkers, and Emerging Targeted Therapies.International journal of molecular sciences · 2026Review
- Structural insights into C3 convertase activity of the classical pathway of complement.Nature communications · 2025Article
- Enzymatic conversion of human blood group A kidneys to universal blood group O.Nature communications · 2024Article
- Storage of Transfusion Platelet Concentrates Is Associated with Complement Activation and Reduced Ability of Platelets to Respond to Protease-Activated Receptor-1 and Thromboxane A2 Receptor.International journal of molecular sciences · 2024Article
- The Acquisition of Complement-Dependent Cytotoxicity by the Type II Anti-CD20 Therapeutic Antibody Obinutuzumab.Cancers · 2023Article
- Substitutions at position 263 within the von Willebrand factor type A domain determine the functionality of complement C2 protein.Frontiers in immunology · 2022Article
- A novel biomimetic nanomedicine system with anti-inflammatory and anti-osteoporosis effects improves the therapy efficacy of steroid-resistant nephrotic syndrome.Journal of nanobiotechnology · 2021Article
- Article
- Nanobodies Provide Insight into the Molecular Mechanisms of the Complement Cascade and Offer New Therapeutic Strategies.Biomolecules · 2021Review
- Complement C4, Infections, and Autoimmune Diseases.Frontiers in immunology · 2021Review
- Purification of Human Complement Component C4 and Sample Preparation for Structural Biology Applications.Methods in molecular biology (Clifton, N.J.) · 2021Article
- A C5a-Immunoglobulin complex in chronic lymphocytic leukemia patients is associated with decreased complement activity.PloS one · 2019Article
- Complement and Bacterial Infections: From Molecular Mechanisms to Therapeutic Applications.Journal of innate immunity · 2018Review
- The structural basis for inhibition of the classical and lectin complement pathways by S. aureus extracellular adherence protein.Protein science : a publication of the Protein Society · 2017Article
- Structure and activation of C1, the complex initiating the classical pathway of the complement cascade.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Complement system in Anti-CD20 mAb therapy for cancer: A mini-review.International journal of immunopathology and pharmacologyReview
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lectin (LP) and classical (CP) pathways are two of the three main activation cascades of the complement system. These pathways start with recognition of different pathogen- or danger-associated molecular patterns and include identical steps of proteolytic activation of complement component C4, formation of the C3 proconvertase C4b2, followed by cleavage of complement component C2 within C4b2 resulting in the C3 convertase C4b2a. Here, we describe the solution structures of the two central complexes of the pathways, C3 proconvertase and C3 convertase, as well as the unbound zymogen C2 obtained by small angle x-ray scattering analysis. We analyzed both native and enzymatically deglycosylated C4b2 and C2 and showed that the resulting structural models were independent of the glycans. The small angle x-ray scattering-derived models suggest a different activation mode for the CP/LP C3 proconvertase as compared with that established for the alternative pathway proconvertase C3bB. This is likely due to the rather different structural and functional properties of the proteases activating the proconvertases. The solution structure of a stabilized form of the active CP/LP C3 convertase C4b2a is strikingly similar to the crystal structure of the alternative pathway C3 convertase C3bBb, which is in accordance with their identical functions in cleaving the complement proteins C3 and C5.
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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.