Experimentally determined long intrinsically disordered protein regions are now abundant in the Protein Data Bank
Experimentally determined long intrinsically disordered protein regions are now abundant in the Protein Data Bank
Abstract Intrinsically disordered protein regions are commonly defined from missing electron density in X-ray structures. Experimental evidence for long disorder regions (LDRs) of at least 30 residues was so far limited to a less than a thousand manually curated proteins. Here, we describe a comprehensive and large-scale analysis of experimental LDRs for 3,133 unique proteins, demonstrating an increasing coverage of intrinsic disorder in the Protein Data Bank (PDB) in the last decade. The results suggest that long missing residue regions are a good quality source to annotate intrinsically disordered regions and perform functional analysis in large data sets. The consensus approach used to define LDRs allows to evaluate context dependent disorder and provide a common definition at the protein level.
Monzon Alexander Miguel、Zanotti Giuseppe、Piovesan Damiano、Tosatto Silvio C. E.、Necci Marco、Walsh Ian、Quaglia Federica
Department of Biomedical Sciences, University of PaduaDepartment of Biomedical Sciences, University of PaduaDepartment of Biomedical Sciences, University of PaduaDepartment of Biomedical Sciences, University of PaduaDepartment of Biomedical Sciences, University of PaduaBioprocessing Technology InstituteDepartment of Biomedical Sciences, University of Padua
生物化学生物物理学分子生物学
intrinsically disordered proteinsprotein flexibilitystructure missing residuesdisordered regions
Monzon Alexander Miguel,Zanotti Giuseppe,Piovesan Damiano,Tosatto Silvio C. E.,Necci Marco,Walsh Ian,Quaglia Federica.Experimentally determined long intrinsically disordered protein regions are now abundant in the Protein Data Bank[EB/OL].(2025-03-28)[2025-05-09].https://www.biorxiv.org/content/10.1101/2020.02.17.952028.点此复制
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