ArticleThe Journal of biological chemistry1992
Probing the phosphocholine-binding site of human C-reactive protein by site-directed mutagenesis.
Article in The Journal of biological chemistry, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The trial behind it
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
17 citing papers in PubMed, 45 citations in OpenAlex.
- Redefining CRP in tissue injury and repair: more than an acute pro-inflammatory mediator.Frontiers in immunology · 2025Review
- Protection against prolonged pneumococcal infection involves structural changes in C-reactive protein and subsequent binding to both phosphocholine and amyloids on the bacterial surface.Frontiers in immunology · 2025Article
- Monomeric C-reactive protein is associated with severity and prognosis of decompensated hepatitis B cirrhosis.Frontiers in immunology · 2024Article
- 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
- Structurally Altered, Not Wild-Type, Pentameric C-Reactive Protein Inhibits Formation of Amyloid-β Fibrils.Journal of immunology (Baltimore, Md. : 1950) · 2022Article
- C-Reactive Protein and Cancer-Diagnostic and Therapeutic Insights.Frontiers in immunology · 2020Review
- Treatment of Pneumococcal Infection by Using Engineered Human C-Reactive Protein in a Mouse Model.Frontiers in immunology · 2020Article
- Hyper-acidic fusion minipeptides escort the intrinsic antioxidative ability of the pattern recognition receptor CRP in non-animal organisms.Scientific reports · 2019Article
- Hydroxycholesterol binds and enhances the anti-viral activities of zebrafish monomeric c-reactive protein isoforms.PloS one · 2019Article
- Exposing a hidden functional site of C-reactive protein by site-directed mutagenesis.The Journal of biological chemistry · 2012Article
- Predicting the disruption by UO2(2+) of a protein-ligand interaction.Protein science : a publication of the Protein Society · 2010Article
- Pattern recognition by pentraxins.Advances in experimental medicine and biology · 2009Review
- Role of the property of C-reactive protein to activate the classical pathway of complement in protecting mice from pneumococcal infection.Journal of immunology (Baltimore, Md. : 1950) · 2006Article
- Interaction of calcium-bound C-reactive protein with fibronectin is controlled by pH: in vivo implications.The Journal of biological chemistry · 2004Article
- Lectin like properties and differential sugar binding characteristics of C-reactive proteins purified from sera of normal and pollutant induced Labeo rohita.Glycoconjugate journal · 1999Article
- Calcium-dependent binding of rabbit C-reactive protein to supported lipid monolayers containing exposed phosphorylcholine group.Biophysical journal · 1999Article
- C-reactive protein: structural biology, gene expression, and host defense function.Immunologic research · 1997Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Human C-reactive protein (CRP) can activate the classical pathway of complement and function as an opsonin only when it is complexed to an appropriate ligand. Most known CRP ligands bind to the phosphocholine (PCh)-binding site of the protein. In the present study, we used oligonucleotide-directed site-specific mutagenesis to investigate structural determinants of the PCh-binding site of CRP. Eight mutant recombinant (r) CRP, Y40F; E42Q; Y40F, E42Q; K57Q; R58G; K57Q, R58G; W67K; and K57Q, R58G, W67K were constructed and expressed in COS cells. Wild-type and all mutant rCRP except for the W67K mutants bound to solid-phase PCh-substituted bovine serum albumin (PCh-BSA) with similar apparent avidities. However, W67K rCRP had decreased avidity for PCh-BSA and the triple mutant, K57Q, R58G, W67K, failed to bind PCh-BSA. Inhibition experiments using PCh and dAMP as inhibitors indicated that both Lys-57 and Arg-58 contribute to PCh binding. They also indicated that Trp-67 provides interactions with the choline group. The Y40F and E42Q mutants were found to have increased avidity for fibronectin compared to wild-type rCRP. We conclude that the residues Lys-57, Arg-58, and Trp-67 contribute to the structure of the PCh-binding site of human CRP. Residues Tyr-40 and Glu-42 do not appear to participate in the formation of the PCh-binding site of CRP, however, they may be located in the vicinity of the fibronectin-binding site of CRP.
Indexed as
Identifiers
1460031PMC5317095W91782350What OpenQuestion holds
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.