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Structural Basis of CD160:HVEM Recognition.

Weifeng Liu1, Sarah C Garrett1, Elena V Fedorov1

  • 1Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.

Structure (London, England : 1993)
|June 25, 2019
PubMed
Summary
This summary is machine-generated.

CD160, a key immune signaling molecule, binds to HVEM. This study reveals the structural basis of their interaction, crucial for understanding immune responses and developing therapies.

Keywords:
CD160 and HVEMIgSF and TNFRSF interactionsInteraction promiscuityT cell costimulation and coinhibitionX-ray structuresimmune regulationintermolecular beta-sheet

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Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Interactions

Background:

  • CD160 is a signaling molecule involved in T cell inhibition, NK cell activation, and mucosal immunity.
  • CD160 interacts with herpes virus entry mediator (HVEM), mediating bidirectional signaling crucial for immune responses.
  • The structural basis of CD160:HVEM engagement remains undescribed despite its therapeutic relevance.

Purpose of the Study:

  • To elucidate the structural and mechanistic basis of the CD160:HVEM interaction.
  • To determine the crystal structures of the human CD160 extracellular domain and its complex with human HVEM.

Main Methods:

  • X-ray crystallography was used to determine the structures of human CD160 extracellular domain and the CD160:HVEM complex.
  • Structural analysis of the CD160 ectodomain and its interaction interface with HVEM.

Main Results:

  • CD160 possesses a unique immunoglobulin fold variation and exists as a monomer.
  • The CD160:HVEM complex forms with a 1:1 stoichiometry.
  • The binding interface of CD160:HVEM is structurally analogous to the BTLA:HVEM complex.

Conclusions:

  • This study provides the first structural insights into the CD160:HVEM recognition mechanism.
  • The findings reveal the determinants governing CD160:HVEM binding and subsequent signaling.
  • Understanding this interaction is vital for targeting immune signaling pathways therapeutically.