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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Calorimetry
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Crystallization
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Crystallography, X-Ray
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Humans
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Models, Molecular
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Molecular Sequence Data
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Protein Binding
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Receptors, TNF-Related Apoptosis-Inducing Ligand / chemistry*
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Receptors, TNF-Related Apoptosis-Inducing Ligand / isolation & purification
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TNF-Related Apoptosis-Inducing Ligand / chemistry*
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TNF-Related Apoptosis-Inducing Ligand / isolation & purification
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Thermodynamics
Substances
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Receptors, TNF-Related Apoptosis-Inducing Ligand
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TNF-Related Apoptosis-Inducing Ligand
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TNFRSF10A protein, human
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TNFSF10 protein, human