IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies

Ho Yee Joyce Fung, Melissa Birol, Elizabeth Rhoades

Research output: Contribution to journalReview articlepeer-review

45 Scopus citations

Abstract

Intrinsically disordered proteins (IDPs) have critical roles in a diverse array of cellular functions. Of relevance here is that they are components of macromolecular complexes, where their conformational flexibility helps mediate interactions with binding partners. IDPs often interact with their binding partners through short sequence motifs, commonly repeated within the disordered regions. As such, multivalent interactions are common for IDPs and their binding partners within macromolecular complexes. Here we discuss the importance of IDP multivalency in three very different macromolecular assemblies: biomolecular condensates, the nuclear pore, and the cytoskeleton.

Original languageEnglish (US)
Pages (from-to)36-43
Number of pages8
JournalCurrent Opinion in Structural Biology
Volume49
DOIs
StatePublished - Apr 2018
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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