ArticleActa crystallographica. Section D, Biological crystallography2014
Structural and functional characterization of human and murine C5a anaphylatoxins.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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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Who cites it
19 citing papers in PubMed, 54 citations in OpenAlex.
- A novel long-acting C5a-blocking cyclic peptide prevents sepsis-induced organ dysfunction via effective blockade of the inflammatory cascade.Signal transduction and targeted therapy · 2025Article
- State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025Review
- Biophysical and structural studies of fibulin-2.Scientific reports · 2024Article
- Revealing the signaling of complement receptors C3aR and C5aR1 by anaphylatoxins.Nature chemical biology · 2023Article
- Molecular basis of anaphylatoxin binding, activation, and signaling bias at complement receptors.Cell · 2023Article
- Heat-inactivated Factor B inhibits alternative pathway fluid-phase activation and convertase formation on endothelial cell-secreted ultra-large von Willebrand factor strings.Scientific reports · 2023Article
- Mechanism of activation and biased signaling in complement receptor C5aR1.Cell research · 2023Article
- The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2021Review
- In vitro and in vivo safety studies indicate that R15, a synthetic polyarginine peptide, could safely reverse the effects of unfractionated heparin.FEBS open bio · 2021Article
- Carboxypeptidase B blocks ex vivo activation of the anaphylatoxin-neutrophil extracellular trap axis in neutrophils from COVID-19 patients.Critical care (London, England) · 2021Article
- Partial ligand-receptor engagement yields functional bias at the human complement receptor, C5aR1.The Journal of biological chemistry · 2019Article
- The Model Structures of the Complement Component 5a Receptor (C5aR) Bound to the Native and EngineeredScientific reports · 2018Article
- Article
- A novel hemolytic complement-sufficient NSG mouse model supports studies of complement-mediated antitumor activity in vivo.Journal of immunological methods · 2017Article
- Complement activation, regulation, and molecular basis for complement-related diseases.The EMBO journal · 2015Review
- Model structures of inactive and peptide agonist bound C5aR: Insights into agonist binding, selectivity and activation.Biochemistry and biophysics reports · 2015Article
- Structural basis for the targeting of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer.Nature communications · 2015Article
- Complement System Part II: Role in Immunity.Frontiers in immunology · 2015Review
- Complement System Part I - Molecular Mechanisms of Activation and Regulation.Frontiers in immunology · 2015Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complement is an ancient part of the innate immune system that plays a pivotal role in protection against invading pathogens and helps to clear apoptotic and necrotic cells. Upon complement activation, a cascade of proteolytic events generates the complement effectors, including the anaphylatoxins C3a and C5a. Signalling through their cognate G-protein coupled receptors, C3aR and C5aR, leads to a wide range of biological events promoting inflammation at the site of complement activation. The function of anaphylatoxins is regulated by circulating carboxypeptidases that remove their C-terminal arginine residue, yielding C3a-desArg and C5a-desArg. Whereas human C3a and C3a-desArg adopt a canonical four-helix bundle fold, the conformation of human C5a-desArg has recently been described as a three-helix bundle. Here, the crystal structures of an antagonist version of human C5a, A8(Δ71-73), and of murine C5a and C5a-desArg are reported. Whereas A8(Δ71-73) adopts a three-helix bundle conformation similar to human C5a-desArg, the two murine proteins form a four-helix bundle. A cell-based functional assay reveals that murine C5a-desArg, in contrast to its human counterpart, exerts the same level of activition as murine C5a on its cognate receptor. The role of the different C5a conformations is discussed in relation to the differential activation of C5a receptors across species.
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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.