StrIDR: a database of intrinsically disordered regions of proteins with experimentally resolved structures

Abstract

AbstractMotivationIntrinsically disordered regions (IDRs) of proteins exist as an ensemble of conformations, and not as a single structure. Existing databases contain extensive, experimentally derived annotations of intrinsic disorder for millions of proteins at the sequence level. However, only a tiny fraction of these IDRs are associated with an experimentally determined protein structure. Moreover, even if a structure exists, parts of the disordered regions may still be unresolved.ResultsHere we organizeStructures ofIntrinsicallyDisorderedRegions (StrIDR), a database of IDRs confirmedviaexperimental or homology-based evidence, resolved in experimentally determined structures. The database can provide useful insights into the dynamics, folding, and interactions of IDRs. It can also facilitate computational studies on IDRs, such as those using molecular dynamics simulations and/or machine learning.AvailabilityStrIDR is available athttps://isblab.ncbs.res.in/stridr. The web UI allows for downloading PDB structures and SIFTS mappings of individual entries. Additionally, the entire database can be downloaded in a JSON format. The source code for creating and updating the database is available athttps://github.com/isblab/stridr.