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Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank.
Monzon, Alexander Miguel; Necci, Marco; Quaglia, Federica; Walsh, Ian; Zanotti, Giuseppe; Piovesan, Damiano; Tosatto, Silvio C E.
Afiliación
  • Monzon AM; Department of Biomedical Sciences, University of Padua, 35131 Padua, Italy.
  • Necci M; Department of Biomedical Sciences, University of Padua, 35131 Padua, Italy.
  • Quaglia F; Department of Biomedical Sciences, University of Padua, 35131 Padua, Italy.
  • Walsh I; Bioprocessing Technology Institute, A*STAR, Singapore 138668, Singapore.
  • Zanotti G; Department of Biomedical Sciences, University of Padua, 35131 Padua, Italy.
  • Piovesan D; Department of Biomedical Sciences, University of Padua, 35131 Padua, Italy.
  • Tosatto SCE; Department of Biomedical Sciences, University of Padua, 35131 Padua, Italy.
Int J Mol Sci ; 21(12)2020 Jun 24.
Article en En | MEDLINE | ID: mdl-32599863
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 manually curated proteins. Here, we describe a comprehensive and large-scale analysis of experimental LDRs for 3133 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.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Modelos Moleculares / Biología Computacional / Bases de Datos de Proteínas / Proteínas Intrínsecamente Desordenadas Límite: Animals / Humans Idioma: En Revista: Int J Mol Sci Año: 2020 Tipo del documento: Article País de afiliación: Italia

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Modelos Moleculares / Biología Computacional / Bases de Datos de Proteínas / Proteínas Intrínsecamente Desordenadas Límite: Animals / Humans Idioma: En Revista: Int J Mol Sci Año: 2020 Tipo del documento: Article País de afiliación: Italia