Authors

Damiano Piovesan, University of Padova
Francesco Tabaro, University of Padova
Ivan Mičetić, University of Padova
Marco Necci, University of Padova
Federica Quaglia, University of Padova
Christopher J. Oldfield, Indiana University School of Medicine
Maria Cristina Aspromonte, University of Padova
Norman E. Davey, Conway Institute of Biomolecular & Biomedical Research
Radoslav Davidović, Institute of Nuclear Sciences Vinca
Zsuzsanna Dosztányi, Eötvös Loránd University
Arne Elofsson, Stockholm University
Alessandra Gasparini, University of Padova
András Hatos, University of Padova
Andrey V. Kajava, Centre de Recherche en Biologie cellulaire de Montpellier (CRBM), UMR 5237 CNRS, Université Montpellier 1919 Route de Mende, Cedex 5, Montpellier 34293, France
Lajos Kalmar, Institute of Enzymology
Emanuela Leonardi, University of Padova
Tamas Lazar, Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels 1050, Belgium
Sandra Macedo-Ribeiro, 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
Mauricio Macossay-Castillo, Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels 1050, Belgium
Attila Meszaros, Institute of Enzymology
Giovanni Minervini, University of Padova
Nikoletta Murvai, Institute of Enzymology
Jordi Pujols, Departament de Bioquimica i Biologia Molecular and Institut de Biotecnologia i Biomedicina, Universitat Autònoma de Barcelona, Bellaterra 08193, Spain
Daniel B. Roche, Centre de Recherche en Biologie cellulaire de Montpellier (CRBM), UMR 5237 CNRS, Université Montpellier 1919 Route de Mende, Cedex 5, Montpellier 34293, France
Edoardo Salladini, Aix-Marseille Univ, CNRS, AFMB, UMR 7257, Marseille, France
Eva Schad, Institute of Enzymology
Antoine Schramm, Aix-Marseille Univ, CNRS, AFMB, UMR 7257, Marseille, France
Beata Szabo, Institute of Enzymology
Agnes Tantos, Institute of Enzymology
Fiorella Tonello, University of Padova
Konstantinos D. Tsirigos, Stockholm University
Nevena Veljković, Institute of Nuclear Sciences Vinca
Salvador Ventura, Universitat Autònoma de Barcelona
Wim Vranken, Structural Biology Brussels, Vrije Universiteit Brussel (VUB), Brussels 1050, Belgium
Per Warholm, Stockholm University
Vladimir N. Uversky, University of South FloridaFollow
A. Keith Dunker, Indiana University School of Medicine
Sonia Longhi, Aix-Marseille Univ, CNRS, AFMB, UMR 7257, Marseille, France
Peter Tompa, Institute of Enzymology
Silvio C.E. Tosatto, University of Padova

Document Type

Article

Publication Date

2017

Keywords

nuclear magnetic resonance, community

Digital Object Identifier (DOI)

https://doi.org/10.1093/nar/gkw1056

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.

Rights Information

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial 4.0 License

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Nucleic Acids Research, v. 45, issue D1, p. D219-D227

Share

COinS