ArticleThe Journal of biological chemistry2008
Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 63 citations in OpenAlex.
- Iron chaperones and RNA-binding proteins, PCBP1 and PCBP2, maintain hepatic iron balance and protect against ferroptosis.Free radical biology & medicine · 2026Article
- Structure, function, regulation, evolution, and therapeutic implications of PARP14.Genes & development · 2026Review
- Indirect identification of genomic G-quadruplexes via a small protein probe that specifically recognizes C-rich single-stranded DNA.Nucleic acids research · 2026Article
- Colorectal cancer-associated PCBP1 mutations disrupt protein stability in a dominant negative manner.bioRxiv : the preprint server for biology · 2025Article
- The dual role of RNA-binding proteins: promotion of tumorigenesis, drug resistance, and emerging therapeutic targets.Acta biochimica et biophysica Sinica · 2025Article
- A sequence-specific RNA acetylation catalyst.Nucleic acids research · 2025Article
- A minimal complex of KHNYN and zinc-finger antiviral protein binds and degrades single-stranded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A sequence-specific RNA acetylation catalyst.bioRxiv : the preprint server for biology · 2024Article
- Structural basis for cloverleaf RNA-initiated viral genome replication.Nucleic acids research · 2023Article
- Structural Characteristics of the 5'-Terminal Region of Mouse p53 mRNA and Identification of Proteins That Bind to This mRNA Region.International journal of molecular sciences · 2022Article
- The androgen receptor messenger RNA: what do we know?RNA biology · 2022Review
- Poly(C)-binding Protein 2 Regulates the p53 Expression via Interactions with the 5'-Terminal Region of p53 mRNA.International journal of molecular sciences · 2021Article
- Efficient translation of Eggplant mottled dwarf nucleorhabdovirus N and X genes requires both 5' and 3' UTRs.Virology journal · 2021Article
- easyCLIP analysis of RNA-protein interactions incorporating absolute quantification.Nature communications · 2021Article
- The importance of CDC27 in cancer: molecular pathology and clinical aspects.Cancer cell international · 2021Review
- Molecular characterization of the RNA-protein complex directing -2/-1 programmed ribosomal frameshifting during arterivirus replicase expression.The Journal of biological chemistry · 2020Article
- Structure of the PCBP2/stem-loop IV complex underlying translation initiation mediated by the poliovirus type I IRES.Nucleic acids research · 2020Article
- Specific binding of PCBP1 to heavily oxidized RNA to induce cell death.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer.The Journal of biological chemistry · 2017Article
- PCBP2 enables the cadicivirus IRES to exploit the function of a conserved GRNA tetraloop to enhance ribosomal initiation complex formation.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Poly(C)-binding proteins (PCBPs) are important regulatory proteins that contain three KH (hnRNP K homology) domains. Binding poly(C) D/RNA sequences via KH domains is essential for multiple PCBP functions. To reveal the basis for PCBP-D/RNA interactions and function, we determined the structure of a construct containing the first two domains (KH1-KH2) of human PCBP2 by NMR. KH1 and KH2 form an intramolecular pseudodimer. The large hydrophobic dimerization surface of each KH domain is on the side opposite the D/RNA binding interface. Chemical shift mapping indicates both domains bind poly(C) DNA motifs without disrupting the KH1-KH2 interaction. Spectral comparison of KH1-KH2, KH3, and full-length PCBP2 constructs suggests that the KH1-KH2 pseudodimer forms, but KH3 does not interact with other parts of the protein. From NMR studies and modeling, we propose possible modes of cooperative binding tandem poly(C) motifs by the KH domains. D/RNA binding may induce pseudodimer dissociation or stabilize dissociated KH1 and KH2, making protein interaction surfaces available to PCBP-binding partners. This conformational change may represent a regulatory mechanism linking D/RNA binding to PCBP functions.
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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.