Premium
The structure of the death receptor 4–TNF‐related apoptosis‐inducing ligand (DR4–TRAIL) complex
Author(s) -
Ramamurthy Vidhyashankar,
Yamniuk Aaron P.,
Lawrence Eric J.,
Yong Wei,
Schneeweis Lumelle A.,
Cheng Lin,
Murdock Melissa,
Corbett Martin J.,
Doyle Michael L.,
Sheriff Steven
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15016416
Subject(s) - apoptosis , ligand (biochemistry) , receptor , tumor necrosis factor alpha , similarity (geometry) , chemistry , microbiology and biotechnology , stereochemistry , biology , immunology , biochemistry , computer science , artificial intelligence , image (mathematics)
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.