Aims to serve as a starting point for functional and structural analysis of interactions between intrinsically Disordered Proteins (IDPs). MFIB is based on the integration of structural and sequence annotation coupled with the results of an extensive manual literature survey. The data contained in MFIB provide a wide coverage of possible IDP-IDP interactions in many ways. Its entries cover the majority of possible oligomeric compositions from dimers to hexamers, including both hetero- and homo-oligomers.
A community resource for pre-computed disorder predictions on a large library of proteins from completely-sequenced genomes. Goals of the database include making statistical comparisons of the various prediction methods freely available to the prediction community, as well as facilitating biological investigation of the disordered protein space.
Annotates protein sequences for intrinsically disorder regions from the literature. DisProt classifies intrinsic disorder based on experimental methods and three ontologies for molecular function, transition and binding partner. It holds information on more than 800 entries of intrinsically disordered proteins (IDPs) or regions (IDRs) that exist and function without a well-defined three-dimensional structure. The assessment of disorder is based 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 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.
Provides an ultimate resource for functional site classifications in intrinsically disordered proteins (IDPs). DisBind is a database dedicated to residue-level classification of functional binding sites in disordered and structured regions of intrinsically disordered proteins. This resource compiles information from the structural database (protein databank), the database of experimentally validated disordered proteins (DisProt), and the comprehensive protein sequence and functional database (UniProt).
Serves as an openly accessible database for the deposition of structural ensembles of intrinsically disordered proteins (IDPs) and of denatured proteins based on nuclear magnetic resonance spectroscopy, small-angle X-ray scattering and other data measured in solution. PE-DB is open for submissions from the community, and is intended as a forum for disseminating the structural ensembles and the methodologies used to generate them. While the need to represent the IDP structures is clear, methods for determining and evaluating the structural ensembles are still evolving. The availability of the pE-DB database is expected to promote the development of new modeling methods and leads to a better understanding of how function arises from disordered states.
Provides an extensive collection of interactions formed by a disordered protein region and one or more ordered protein partners. DIBS marks proteins as disordered if a closely homologous protein was described to lack intrinsic structure. This application incorporates annotations about functional motifs in disordered partners, further connecting the two complementary models of such interactions. It also serves as the basis for a more complete understanding of Intrinsically Disordered Proteins (IDPs) interactions.
A collection of intrinsically disordered proteins (IDPs) that cannot adopt stable globular structures under physiological conditions. IDEAL incorporates the interactions of IDPs and their binding partners explicitly, and illustrates the protein-protein interaction (PPI) networks and the structures of protein complexes.