Anatomy of β-strands at protein-protein interfaces

Andrew M. Watkins, Paramjit Arora

Research output: Contribution to journalArticle

Abstract

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
Volume9
Issue number8
DOIs
StatePublished - Aug 15 2014

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Anatomy
Proteins
Molecular recognition
Databases
Guidelines
Ligands

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Medicine(all)

Cite this

Anatomy of β-strands at protein-protein interfaces. / Watkins, Andrew M.; Arora, Paramjit.

In: ACS Chemical Biology, Vol. 9, No. 8, 15.08.2014, p. 1747-1754.

Research output: Contribution to journalArticle

Watkins, Andrew M. ; Arora, Paramjit. / Anatomy of β-strands at protein-protein interfaces. In: ACS Chemical Biology. 2014 ; Vol. 9, No. 8. pp. 1747-1754.
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