Author:
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
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.
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
Cited by
26 articles.
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