Redesigning HVEM Interface for Selective Binding to LIGHT, BTLA, and CD160

Rojan Shrestha, Sarah C. Garrett-Thomson, Weifeng Liu, Steven C. Almo, Andras Fiser

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Shrestha et al. use a residue-based pharmacophore as a computational approach to design mutations for the interface of HVEM to make it selective to one or two of its three cognate ligands. In cell assay experiments, 15 of the 25 designed single and double point mutants proved to introduce statistically significant selectivity.

Original languageEnglish (US)
Pages (from-to)1197-1205.e2
JournalStructure
Volume28
Issue number11
DOIs
StatePublished - Nov 3 2020

Keywords

  • HVEM
  • ProtLID
  • computational interface design
  • immune synapse
  • protein-based drug discovery
  • protein-protein interactions
  • residue-specific pharmacophores
  • switchable-binding selectivity

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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