ArticleActa crystallographica. Section D, Biological crystallography2009
The structure of C2b, a fragment of complement component C2 produced during C3 convertase formation.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- The Immuno-Glial Connectome in Alzheimer's Disease: Integrating Central and Peripheral Inflammatory Networks.Cellular and molecular neurobiology · 2026Review
- Structural insights into C3 convertase activity of the classical pathway of complement.Nature communications · 2025Article
- The Complement System.Advances in experimental medicine and biology · 2025Review
- Article
- DNA Nanostructure-Templated Antibody Complexes Provide Insights into the Geometric Requirements of Human Complement Cascade Activation.Journal of the American Chemical Society · 2024Article
- Investigation of Potential Drug Targets Involved in Inflammation Contributing to Alzheimer's Disease Progression.Pharmaceuticals (Basel, Switzerland) · 2024Review
- The Acquisition of Complement-Dependent Cytotoxicity by the Type II Anti-CD20 Therapeutic Antibody Obinutuzumab.Cancers · 2023Article
- In Silico Designed Gain-of-Function Variants of Complement C2 Support Cytocidal Activity of Anticancer Monoclonal Antibodies.Cancers · 2022Article
- Substitutions at position 263 within the von Willebrand factor type A domain determine the functionality of complement C2 protein.Frontiers in immunology · 2022Article
- Complement System in Alzheimer's Disease.International journal of molecular sciences · 2021Review
- Review
- Treatment of Rare Inflammatory Kidney Diseases: Drugs Targeting the Terminal Complement Pathway.Frontiers in immunology · 2020Review
- Review
- Proteomics in gastroparesis: unique and overlapping protein signatures in diabetic and idiopathic gastroparesis.American journal of physiology. Gastrointestinal and liver physiology · 2019Article
- Exome sequencing in multiple sclerosis families identifies 12 candidate genes and nominates biological pathways for the genesis of disease.PLoS genetics · 2019Article
- 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
- Novel Evasion Mechanisms of the Classical Complement Pathway.Journal of immunology (Baltimore, Md. : 1950) · 2016Review
- Solution Structures of Complement C2 and Its C4 Complexes Propose Pathway-specific Mechanisms for Control and Activation of the Complement Proconvertases.The Journal of biological chemistry · 2016Article
- Proteomics Study on Nonallergic Hypersensitivity Induced by Compound 4880 and Ovalbumin.PloS one · 2016Article
- Complement System Part I - Molecular Mechanisms of Activation and Regulation.Frontiers in immunology · 2015Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The second component of complement (C2) is a multi-domain serine protease that provides catalytic activity for the C3 and C5 convertases of the classical and lectin pathways of human complement. The formation of these convertases requires the Mg(2+)-dependent binding of C2 to C4b and the subsequent cleavage of C2 by C1s or MASP2, respectively. The crystal structure of full-length C2 is not yet available, although the structure of its C-terminal catalytic segment C2a has been determined. The crystal structure of the N-terminal segment C2b of C2 determined to 1.8 A resolution presented here reveals the arrangement of its three CCP domains. The domains are arranged differently compared with most other CCP-domain assemblies, but their arrangement is similar to that found in the Ba part of the full-length factor B structure. The crystal structures of C2a, C2b and full-length factor B are used to generate a model for C2 and a discussion of the domain association and possible interactions with C4b during formation of the C4b-C2 complex is presented. The results of this study also suggest that upon cleavage by C1s, C2a domains undergo conformational rotation while bound to C4b and the released C2b domains may remain folded together similar to as observed in the intact protein.
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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.