Anatomy of β-strands at protein-protein interfaces

Andrew M. Watkins, Paramjit S. Arora

Research output: Contribution to journalArticlepeer-review


The development of inhibitors for protein-protein interactions frequently involves the mimicry of secondary structure motifs. While helical protein-protein interactions have been heavily targeted, a similar level of success for the inhibition of β-strand and β-sheet rich interfaces has been elusive. We describe an assessment of the full range of β-strand interfaces whose high-resolution structures are available in the Protein Data Bank. This analysis identifies complexes where a β-stand or β-sheet contributes significantly to binding. The results highlight the molecular recognition complexity in strand-mediated interactions relative to helical interfaces and offer guidelines for the construction of β-strand and β-sheet mimics as ligands for protein receptors. The online data set will potentially serve as an entry-point to new classes of protein-protein interaction inhibitors.

Original languageEnglish (US)
Pages (from-to)1747-1754
Number of pages8
JournalACS Chemical Biology
Issue number8
StatePublished - Aug 15 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine


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