ArticleBiochemistry2006
Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: mutational studies using recombinant globular head modules of human C1q A, B, and C chains.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 143 citations in OpenAlex.
- Article
- Article
- CRP (C-Reactive Protein) Revisited: An Old Yet New Biomarker of Acute and Chronic Inflammation.Cells · 2026Review
- Young adult microglial deletion of C1q reduces engulfment of synapses and prevents cognitive impairment in an aggressive Alzheimer's disease mouse model.bioRxiv : the preprint server for biology · 2025Article
- C-reactive protein: the nexus between inflammation and protein misfolding diseases.Frontiers in immunology · 2025Review
- The Complement System.Advances in experimental medicine and biology · 2025Review
- The long pentraxin 3: the invisible loom weaving the warp and weft of tumor destiny.Frontiers in immunology · 2025Review
- Severe COVID-19 induces prolonged elevation of the acute-phase protein pentraxin 3.Frontiers in immunology · 2025Article
- Therapeutic antibodies in oncology: an immunopharmacological overview.Cancer immunology, immunotherapy : CII · 2024Review
- Structural basis for surface activation of the classical complement cascade by the short pentraxin C-reactive protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Selection and characterization of a peptide-based complement modulator targeting C1 of the innate immune system.RSC chemical biology · 2024Article
- PolySialic Acid Nanoparticles Actuate Complement-Factor-H-Mediated Inhibition of the Alternative Complement Pathway: A Safer Potential Therapy for Age-Related Macular Degeneration.Pharmaceuticals (Basel, Switzerland) · 2024Article
- PTX3 structure determination using a hybrid cryoelectron microscopy and AlphaFold approach offers insights into ligand binding and complement activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Relevance of lipoproteins, membranes, and extracellular vesicles in understanding C-reactive protein biochemical structure and biological activities.Frontiers in cardiovascular medicine · 2022Review
- In Vitro and In Silico Interaction Studies with Red Wine Polyphenols against Different Proteins from Human Serum.Molecules (Basel, Switzerland) · 2021Article
- Nanobodies Provide Insight into the Molecular Mechanisms of the Complement Cascade and Offer New Therapeutic Strategies.Biomolecules · 2021Review
- New Insights on the Role of pentraxin-3 in Allergic Asthma.Frontiers in allergy · 2021Review
- The Phagocytic Code Regulating Phagocytosis of Mammalian Cells.Frontiers in immunology · 2021Review
- Perspectives on long pentraxin 3 and rheumatoid arthritis: several potential breakthrough points relying on study foundation of the past.International journal of medical sciences · 2021Review
3 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
Abstract
C1q is the first subcomponent of the classical complement pathway that can interact with a range of biochemically and structurally diverse self and nonself ligands. The globular domain of C1q (gC1q), which is the ligand-recognition domain, is a heterotrimeric structure composed of the C-terminal regions of A (ghA), B (ghB), and C (ghC) chains. The expression and functional characterization of ghA, ghB, and ghC modules have revealed that each chain has specific and differential binding properties toward C1q ligands. It is largely considered that C1q-ligand interactions are ionic in nature; however, the complementary ligand-binding sites on C1q and the mechanisms of interactions are still unclear. To identify the residues on the gC1q domain that are likely to be involved in ligand recognition, we have generated a number of substitution mutants of ghA, ghB, and ghC modules and examined their interactions with three selected ligands: IgG1, C-reactive protein (CRP), and pentraxin 3 (PTX3). Our results suggest that charged residues belonging to the apex of the gC1q heterotrimer (with participation of all three chains) as well as the side of the ghB are crucial for C1q binding to these ligands, and their contribution to each interaction is different. It is likely that a set of charged residues from the gC1q surface participate via different ionic and hydrogen bonds with corresponding residues from the ligand, instead of forming separate binding sites. Thus, a recently proposed model suggesting the rotation of the gC1q domain upon ligand recognition may be extended to C1q interaction with CRP and PTX3 in addition to IgG1.
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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.