The structure of the death receptor 4-TNF-related apoptosis-inducing ligand (DR4-TRAIL) complex

Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1273-81. doi: 10.1107/S2053230X15016416. Epub 2015 Sep 23.

Abstract

The structure of death receptor 4 (DR4) in complex with TNF-related apoptosis-inducing ligand (TRAIL) has been determined at 3 Å resolution and compared with those of previously determined DR5-TRAIL complexes. Consistent with the high sequence similarity between DR4 and DR5, the overall arrangement of the DR4-TRAIL complex does not differ substantially from that of the DR5-TRAIL complex. However, subtle differences are apparent. In addition, solution interaction studies were carried out that show differences in the thermodynamics of binding DR4 or DR5 with TRAIL.

Keywords: TNF-related apoptosis-inducing ligand; death receptor 4; death receptor 5.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Calorimetry
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Receptors, TNF-Related Apoptosis-Inducing Ligand / chemistry*
  • Receptors, TNF-Related Apoptosis-Inducing Ligand / isolation & purification
  • TNF-Related Apoptosis-Inducing Ligand / chemistry*
  • TNF-Related Apoptosis-Inducing Ligand / isolation & purification
  • Thermodynamics

Substances

  • Receptors, TNF-Related Apoptosis-Inducing Ligand
  • TNF-Related Apoptosis-Inducing Ligand
  • TNFRSF10A protein, human
  • TNFSF10 protein, human

Associated data

  • PDB/5CIR