ArticleACS omega2020
Identification of Intrinsic Disorder in Complexes from the Protein Data Bank.
Article in ACS omega, 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, 27 citations in OpenAlex.
- AlphaFold-Multimer accurately captures interactions and dynamics of intrinsically disordered protein regions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- HybridDBRpred: improved sequence-based prediction of DNA-binding amino acids using annotations from structured complexes and disordered proteins.Nucleic acids research · 2024Article
- IRAA: A statistical tool for investigating a protein-protein interaction interface from multiple structures.Protein science : a publication of the Protein Society · 2023Article
- Comparative evaluation of AlphaFold2 and disorder predictors for prediction of intrinsic disorder, disorder content and fully disordered proteins.Computational and structural biotechnology journal · 2023Article
- Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions.Biomolecules · 2022Article
- Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins.International journal of molecular sciences · 2021Article
- The protein disorder cycle.Biophysical reviews · 2021Review
- Critical assessment of protein intrinsic disorder prediction.Nature methods · 2021Article
- DescribePROT: database of amino acid-level protein structure and function predictions.Nucleic acids research · 2021Article
- Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIntrinsically disordered proteins or regions (IDPs or IDRs) lack stable structures in solution, yet often fold upon binding with partners. IDPs or IDRs are highly abundant in all proteomes and represent a significant modification of sequence → structure → function paradigm. The Protein Data Bank (PDB) includes complexes containing disordered segments bound to globular proteins, but the molecular mechanisms of such binding interactions remain largely unknown.
resultsIn this study, we present the results of various disorder predictions on a nonredundant set of PDB complexes. In contrast to their structural appearances, many PDB proteins were predicted to be disordered when separated from their binding partners. These predicted-to-be-disordered proteins were observed to form structures depending upon various factors, including heterogroup binding, protein/DNA/RNA binding, disulfide bonds, and ion binding.
conclusionsThis study collects many examples of disorder-to-order transition in IDP complex formation, thus revealing the unusual structure-function relationships of IDPs and providing an additional support for the newly proposed paradigm of the sequence → IDP/IDR ensemble → function.
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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.