ArticleJournal of structural biology2013
An assignment of intrinsically disordered regions of proteins based on NMR structures.
Article in Journal of structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Seq2Bind webserver for binding site prediction from sequences using fine-tuned protein language models.NAR genomics and bioinformatics · 2025Article
- Characterization of Intrinsically Disordered Proteins in Healthy and Diseased States by Nuclear Magnetic Resonance.Reviews on recent clinical trials · 2024Review
- Resolving Dynamics in the Ensemble: Finding Paths through Intermediate States and Disordered Protein Structures.The journal of physical chemistry. B · 2021Article
- Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR.Scientific reports · 2020Article
- Dark Proteome Database: Studies on Disorder.High-throughput · 2020Article
- Molecular Dynamics Ensemble Refinement of Intrinsically Disordered Peptides According to Deconvoluted Spectra from Circular Dichroism.Biophysical journal · 2020Article
- UsingProtein science : a publication of the Protein Society · 2018Article
- Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions.Cellular and molecular life sciences : CMLS · 2017Review
- Order, Disorder, and Everything in Between.Molecules (Basel, Switzerland) · 2016Review
- Unexpected features of the dark proteome.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.International journal of molecular sciences · 2015Article
- An optimized NIntrinsically disordered proteins · 2015Article
- Assessment of protein disorder region predictions in CASP10.Proteins · 2014Article
- IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners.Nucleic acids research · 2014Article
- Digested disorder: Quarterly intrinsic disorder digest (January/February/March, 2013).Intrinsically disordered proteinsReview
- Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Intrinsically disordered proteins (IDPs) do not adopt stable three-dimensional structures in physiological conditions, yet these proteins play crucial roles in biological phenomena. In most cases, intrinsic disorder manifests itself in segments or domains of an IDP, called intrinsically disordered regions (IDRs), but fully disordered IDPs also exist. Although IDRs can be detected as missing residues in protein structures determined by X-ray crystallography, no protocol has been developed to identify IDRs from structures obtained by Nuclear Magnetic Resonance (NMR). Here, we propose a computational method to assign IDRs based on NMR structures. We compared missing residues of X-ray structures with residue-wise deviations of NMR structures for identical proteins, and derived a threshold deviation that gives the best correlation of ordered and disordered regions of both structures. The obtained threshold of 3.2Å was applied to proteins whose structures were only determined by NMR, and the resulting IDRs were analyzed and compared to those of X-ray structures with no NMR counterpart in terms of sequence length, IDR fraction, protein function, cellular location, and amino acid composition, all of which suggest distinct characteristics. The structural knowledge of IDPs is still inadequate compared with that of structured proteins. Our method can collect and utilize IDRs from structures determined by NMR, potentially enhancing the understanding of IDPs.
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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.