Identification of Intrinsic Disorder in Complexes from the Protein Data Bank

Jianhong Zhou, Christopher J. Oldfield, Wenying Yan, Bairong Shen, A. Keith Dunker

Research output: Contribution to journalArticle

Abstract

Background: Intrinsically disordered proteins or regions (IDPs or IDRs) lack stable structures in solution, yet often fold upon binding with partners. IDPs or IDRs are highly abundant in all proteomes and represent a significant modification of sequence → structure → function paradigm. The Protein Data Bank (PDB) includes complexes containing disordered segments bound to globular proteins, but the molecular mechanisms of such binding interactions remain largely unknown. Results: In this study, we present the results of various disorder predictions on a nonredundant set of PDB complexes. In contrast to their structural appearances, many PDB proteins were predicted to be disordered when separated from their binding partners. These predicted-to-be-disordered proteins were observed to form structures depending upon various factors, including heterogroup binding, protein/DNA/RNA binding, disulfide bonds, and ion binding. Conclusions: This study collects many examples of disorder-to-order transition in IDP complex formation, thus revealing the unusual structure-function relationships of IDPs and providing an additional support for the newly proposed paradigm of the sequence → IDP/IDR ensemble → function.

Original languageEnglish (US)
Pages (from-to)17883-17891
Number of pages9
JournalACS Omega
Volume5
Issue number29
DOIs
StatePublished - Jul 28 2020

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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