ArticleNature2006
Structure of C3b reveals conformational changes that underlie complement activity.
Article in Nature, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 182 papers, 1 of them a synthesis that pooled it.
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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
182 citing papers in PubMed, 1 synthesis or guideline pooled it, 371 citations in OpenAlex.
- Association between genetic variation of complement C3 and the susceptibility to advanced age-related macular degeneration: a meta-analysis.BMC ophthalmology · 2018Pooled it
- Article
- Glycoproteomic and genetic analysis of N-glycosylation of complement component C3 reveals immune pathway regulation.Genome biology · 2026Article
- Liposomes in tumor treatment: a double-edged sword.Science China. Life sciences · 2026Review
- Advances in cryo-EM that have shaped mechanistic models of membrane-attack-complex assembly and regulation.IUCrJ · 2026Review
- The C-terminal domain of Staphylococcus aureus Efb recruits FHR-2 to C3b, synergistically inhibiting the terminal complement pathway.Journal of immunology (Baltimore, Md. : 1950) · 2026Article
- Complement C3 recognition by C3 convertases.Science advances · 2026Article
- Complement in acute kidney injury: a convergent pathogenic pathway in multifactorial renal damage.Frontiers in immunology · 2026Review
- Intracellular C3 regulates the immune response to infection via NF-κB signaling.Cellular and molecular life sciences : CMLS · 2025Article
- Structural insights into C3 convertase activity of the classical pathway of complement.Nature communications · 2025Article
- Thioester-Containing Protein TEP27 inInternational journal of molecular sciences · 2025Article
- Article
- Proteolytic profiling of human plasma reveals an immunoactive complement C3 fragment.The EMBO journal · 2025Article
- Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring.Nature structural & molecular biology · 2025Article
- Knowing the enemy: strategic targeting of complement to treat Alzheimer disease.Nature reviews. Neurology · 2025Review
- Article
- C3 mutations and poor pegcetacoplan response in paroxysmal nocturnal hemoglobinuria.Frontiers in immunology · 2025Article
- The Complement System.Advances in experimental medicine and biology · 2025Review
- A novel and rapid method to purify the human complement opsonin C3b from human plasma.Frontiers in immunology · 2025Article
- Roodmus: a toolkit for benchmarking heterogeneous electron cryo-microscopy reconstructions.IUCrJ · 2024Article
122 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resistance to infection and clearance of cell debris in mammals depend on the activation of the complement system, which is an important component of innate and adaptive immunity. Central to the complement system is the activated form of C3, called C3b, which attaches covalently to target surfaces to amplify complement response, label cells for phagocytosis and stimulate the adaptive immune response. C3b consists of 1,560 amino-acid residues and has 12 domains. It binds various proteins and receptors to effect its functions. However, it is not known how C3 changes its conformation into C3b and thereby exposes its many binding sites. Here we present the crystal structure at 4-A resolution of the activated complement protein C3b and describe the conformational rearrangements of the 12 domains that take place upon proteolytic activation. In the activated form the thioester is fully exposed for covalent attachment to target surfaces and is more than 85 A away from the buried site in native C3 (ref. 5). Marked domain rearrangements in the alpha-chain present an altered molecular surface, exposing hidden and cryptic sites that are consistent with known putative binding sites of factor B and several complement regulators. The structural data indicate that the large conformational changes in the proteolytic activation and regulation of C3 take place mainly in the first conversion step, from C3 to C3b. These insights are important for the development of strategies to treat immune disorders that involve complement-mediated inflammation.
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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.