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.
Vidhyashankar Ramamurthy  1 ,  Aaron P Yamniuk  2 ,  Eric J Lawrence  2 ,  Wei Yong  1 ,  Lumelle A Schneeweis  2 ,  Lin Cheng  2 ,  Melissa Murdock  2 ,  Martin J Corbett  2 ,  Michael L Doyle  2 ,  Steven Sheriff  1
Affiliations
  • 1. Molecular Structure and Design, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
  • 2. Protein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
PMID: 26457518 DOI: 10.1107/S2053230X15016416
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.