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Nucleic Acids Res. 2017 Jan 4;45(D1):D219-D227. doi: 10.1093/nar/gkw1056. Epub 2016 Nov 28.

DisProt 7.0: a major update of the database of disordered proteins.

Author information

1
Department of Biomedical Sciences, University of Padova, I-35121 Padova, Italy.
2
Institute of Biosciences and Medical Technology, University of Tampere, Finland.
3
Center for Computational Biology and Bioinformatics, Indiana University School of Medicine, 46202 Indianapolis, IN, USA.
4
Department of Woman and Child Health, University of Padova, I-35128 Padova, Italy.
5
Conway Institute of Biomolecular & Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland.
6
Ireland UCD School of Medicine & Medical Science, University College Dublin, Belfield, Dublin 4, Ireland.
7
Centre for Multidisciplinary Research, Institute of Nuclear Sciences Vinca, University of Belgrade, 11001 Belgrade, Serbia.
8
MTA-ELTE Lendület Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, 1/c Pázmány Péter sétány, 1117 Budapest, Hungary.
9
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, PO Box 7,H-1518 Budapest, Hungary.
10
Department of Biochemistry and Biophysics and Science for Life Laboratory, Stockholm University, Box 1031, 17121 Solna, Sweden.
11
Centre de Recherche en Biologie cellulaire de Montpellier (CRBM), UMR 5237 CNRS, Université Montpellier 1919 Route de Mende, Cedex 5, Montpellier 34293, France.
12
Institut de Biologie Computationnelle (IBC), Montpellier 34095, France.
13
University ITMO, Institute of Bioengineering, St. Petersburg 197101, Russia.
14
Department of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge CB3 0ES, UK.
15
Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels 1050, Belgium.
16
Structural Biology Research Center (SBRC), Flanders Institute for Biotechnology (VIB), Brussels 1050, Belgium.
17
Biomolecular Structure and Function Group, Instituto de Biologia Molecular e Celular (IBMC) and Instituto de Investigação e Inovação em Saúde (i3S), Universidade do Porto, 4200-135 Porto, Portugal.
18
Departament de Bioquimica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Bellaterra 08193, Spain.
19
Aix-Marseille Univ, CNRS, AFMB, UMR 7257, Marseille, France.
20
CNR Institute of Neurosceince, I-35121 Padova, Italy.
21
Interuniversity Institute of Bioinformatics in Brussels (IB2), ULB-VUB, Brussels 1050, Belgium.
22
Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia.
23
Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.
24
Aix-Marseille Univ, CNRS, AFMB, UMR 7257, Marseille, France Sonia.Longhi@afmb.univ-mrs.fr.
25
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, PO Box 7,H-1518 Budapest, Hungary ptompa@vub.ac.be.
26
Department of Biomedical Sciences, University of Padova, I-35121 Padova, Italy silvio.tosatto@unipd.it.

Abstract

The Database of Protein Disorder (DisProt, URL: www.disprot.org) has been significantly updated and upgraded since its last major renewal in 2007. The current release holds information on more than 800 entries of IDPs/IDRs, i.e. intrinsically disordered proteins or regions that exist and function without a well-defined three-dimensional structure. We have re-curated previous entries to purge DisProt from conflicting cases, and also upgraded the functional classification scheme to reflect continuous advance in the field in the past 10 years or so. We define IDPs as proteins that are disordered along their entire sequence, i.e. entirely lack structural elements, and IDRs as regions that are at least five consecutive residues without well-defined structure. We base our assessment of disorder strictly on experimental evidence, such as X-ray crystallography and nuclear magnetic resonance (primary techniques) and a broad range of other experimental approaches (secondary techniques). Confident and ambiguous annotations are highlighted separately. DisProt 7.0 presents classified knowledge regarding the experimental characterization and functional annotations of IDPs/IDRs, and is intended to provide an invaluable resource for the research community for a better understanding structural disorder and for developing better computational tools for studying disordered proteins.

PMID:
27899601
PMCID:
PMC5210544
DOI:
10.1093/nar/gkw1056
[Indexed for MEDLINE]
Free PMC Article

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