β-Strand-mediated interactions of protein domains

Archana S. Bhat, Lisa N. Kinch, Nick V. Grishin

Research output: Contribution to journalArticle

Abstract

Protein domains exist by themselves or in combination with other domains to form complex multidomain proteins. Defining domain boundaries in proteins is essential for understanding their evolution and function but is not trivial. More specifically, partitioning domains that interact by forming a single β-sheet is known to be particularly troublesome for automatic structure-based domain decomposition pipelines. Here, we study edge-to-edge β-strand interactions between domains in a protein chain, to help define the boundaries for some more difficult cases where a single β-sheet spanning over two domains gives an appearance of one. We give a number of examples where β-strands belonging to a single β-sheet do not belong to a single domain and highlight the difficulties of automatic domain parsers on these examples. This work can be used as a baseline for defining domain boundaries in homologous proteins or proteins with similar domain interactions in the future.

Original languageEnglish (US)
JournalProteins: Structure, Function and Bioinformatics
DOIs
StateAccepted/In press - 2020

Keywords

  • domain boundaries
  • domain interactions
  • homology
  • protein domains
  • structural folds
  • β-sheets and strands

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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