ArticleBiophysical journal2014
p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 63 citations in OpenAlex.
- Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution.Nature communications · 2024Article
- A structure-based designed small molecule depletes hRpn13Nature communications · 2024Article
- The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection.Communications biology · 2024Article
- Characterization of Intrinsically Disordered Proteins in Healthy and Diseased States by Nuclear Magnetic Resonance.Reviews on recent clinical trials · 2024Review
- Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range.Open research Europe · 2022Article
- Accurate model of liquid-liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes.Nucleic acids research · 2021Article
- MMM: Integrative ensemble modeling and ensemble analysis.Protein science : a publication of the Protein Society · 2021Article
- Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature.Journal of molecular biology · 2020Article
- Analysis of Protein Disorder Predictions in the Light of a Protein Structural Alphabet.Biomolecules · 2020Article
- Human PCNA Structure, Function and Interactions.Biomolecules · 2020Review
- Multivalent interaction of ESCO2 with the replication machinery is required for sister chromatid cohesion in vertebrates.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The PCNA interaction motifs revisited: thinking outside the PIP-box.Cellular and molecular life sciences : CMLS · 2019Article
- Article
- p15PAF binding to PCNA modulates the DNA sliding surface.Nucleic acids research · 2018Article
- Steric interference from intrinsically disordered regions controls dynamin-related protein 1 self-assembly during mitochondrial fission.Scientific reports · 2018Article
- Developing a molecular dynamics force field for both folded and disordered protein states.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Disentangling polydispersity in the PCNA-p15PAF complex, a disordered, transient and multivalent macromolecular assembly.Nucleic acids research · 2017Article
- Article
- The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil.PloS one · 2017Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present to our knowledge the first structural characterization of the proliferating-cell-nuclear-antigen-associated factor p15(PAF), showing that it is monomeric and intrinsically disordered in solution but has nonrandom conformational preferences at sites of protein-protein interactions. p15(PAF) is a 12 kDa nuclear protein that acts as a regulator of DNA repair during DNA replication. The p15(PAF) gene is overexpressed in several types of human cancer. The nearly complete NMR backbone assignment of p15(PAF) allowed us to measure 86 N-H(N) residual dipolar couplings. Our residual dipolar coupling analysis reveals nonrandom conformational preferences in distinct regions, including the proliferating-cell-nuclear-antigen-interacting protein motif (PIP-box) and the KEN-box (recognized by the ubiquitin ligase that targets p15(PAF) for degradation). In accordance with these findings, analysis of the (15)N R2 relaxation rates shows a relatively reduced mobility for the residues in these regions. The agreement between the experimental small angle x-ray scattering curve of p15(PAF) and that computed from a statistical coil ensemble corrected for the presence of local secondary structural elements further validates our structural model for p15(PAF). The coincidence of these transiently structured regions with protein-protein interaction and posttranslational modification sites suggests a possible role for these structures as molecular recognition elements for p15(PAF).
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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.