ArticleeLife2021
Properdin oligomers adopt rigid extended conformations supporting function.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Complement C3 recognition by C3 convertases.Science advances · 2026Article
- Structural studies offer a framework for understanding the role of properdin in the alternative pathway and beyond.Immunological reviews · 2023Review
- Structure determination of an unstable macromolecular complex enabled by nanobody-peptide bridging.Protein science : a publication of the Protein Society · 2022Article
- Initial properdin binding contributes to alternative pathway activation at the surface of viable and necrotic cells.European journal of immunology · 2022Article
- Global fitting of multiple data frames from SEC-SAXS to investigate the structure of next-generation nanodiscs.Acta crystallographica. Section D, Structural biology · 2022Article
- Complement component C3: A structural perspective and potential therapeutic implications.Seminars in immunology · 2022Review
- A novel assay that characterizes properdin function shows neutrophil-derived properdin has a distinct oligomeric distribution.Frontiers in immunology · 2022Article
- Exploring urine:serum fractional excretion ratios as potential biomarkers for lupus nephritis.Frontiers in immunology · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Properdin stabilizes convertases formed upon activation of the complement cascade within the immune system. The biological activity of properdin depends on the oligomerization state, but whether properdin oligomers are rigid and how their structure links to function remains unknown. We show by combining electron microscopy and solution scattering, that properdin oligomers adopt extended rigid and well-defined conformations which are well approximated by single models of apparent n-fold rotational symmetry with dimensions of 230-360 Å. Properdin monomers are pretzel-shaped molecules with limited flexibility. In solution, properdin dimers are curved molecules, whereas trimers and tetramers are close to being planar molecules. Structural analysis indicates that simultaneous binding through all binding sites to surface-linked convertases is unlikely for properdin trimer and tetramers. We show that multivalency alone is insufficient for full activity in a cell lysis assay. Hence, the observed rigid extended oligomer structure is an integral component of properdin function.
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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.