ArticleFrontiers in immunology2020
Celluar Folding Determinants and Conformational Plasticity of Native C-Reactive Protein.
Article in Frontiers in immunology, 2020. 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.
- Diagnostic and Prognostic Value of miR-574-3p in Acute Pancreatitis: Insights from Bioinformatics and in vitro Studies.Journal of inflammation research · 2026Article
- C-reactive protein: the nexus between inflammation and protein misfolding diseases.Frontiers in immunology · 2025Review
- C-reactive protein lowers the serum level of IL-17, but not TNF-α, and decreases the incidence of collagen-induced arthritis in mice.Frontiers in immunology · 2024Article
- Glutathione: A Samsonian life-sustaining small molecule that protects against oxidative stress, ageing and damaging inflammation.Frontiers in nutrition · 2022Review
- Relevance of lipoproteins, membranes, and extracellular vesicles in understanding C-reactive protein biochemical structure and biological activities.Frontiers in cardiovascular medicine · 2022Review
- Genetically predicted C-reactive protein mediates the association between rheumatoid arthritis and atlantoaxial subluxation.Frontiers in endocrinology · 2022Article
- Effect of the abolition of intersubunit salt bridges on allosteric protein structural dynamics.Chemical science · 2021Article
- Pattern Recognition Proteins: First Line of Defense Against Coronaviruses.Frontiers in immunology · 2021Review
- How C-Reactive Protein Structural Isoforms With Distinctive Bioactivities Affect Disease Progression.Frontiers in immunology · 2020Review
- Conformationally Altered C-Reactive Protein Capable of Binding to Atherogenic Lipoproteins Reduces Atherosclerosis.Frontiers in immunology · 2020Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
C-reactive protein (CRP) is an acute phase reactant secreted by hepatocytes as a pentamer. The structure formation of pentameric CRP has been demonstrated to proceed in a stepwise manner in live cells. Here, we further dissect the sequence determinants that underlie the key steps in cellular folding and assembly of CRP. The initial folding of CRP subunits depends on a leading sequence with a conserved dipeptide that licenses the formation of the hydrophobic core. This drives the bonding of the intra-subunit disulfide requiring a favorable niche largely conferred by a single residue within the C-terminal helix. A conserved salt bridge then mediates the assembly of folded subunits into pentamer. The pentameric assembly harbors a pronounced plasticity in inter-subunit interactions, which may form the basis for a reversible activation of CRP in inflammation. These results provide insights into how sequence constraints are evolved to dictate structure and function of CRP.
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