RT Journal Article
SR Electronic
T1 Experimentally determined long intrinsically disordered protein regions are now abundant in the Protein Data Bank
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.02.17.952028
DO 10.1101/2020.02.17.952028
A1 Monzon, Alexander Miguel
A1 Necci, Marco
A1 Quaglia, Federica
A1 Walsh, Ian
A1 Piovesan, Damiano
A1 Zanotti, Giuseppe
A1 Tosatto, Silvio C. E.
YR 2020
UL http://biorxiv.org/content/early/2020/02/17/2020.02.17.952028.abstract
AB 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 a less than a thousand manually curated proteins. Here, we describe a comprehensive and large-scale analysis of experimental LDRs for 3,133 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.IDRintrinsically disordered regions;IDPintrinsically disordered protein;LDRlong disordered region.