5cir
From Proteopedia
Crystal structure of death receptor 4 (DR4; TNFFRSF10A) bound to TRAIL (TNFSF10)
Structural highlights
Function[TNF10_HUMAN] Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG. Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis. [TR10A_HUMAN] Receptor for the cytotoxic ligand TNFSF10/TRAIL. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B.[1] Publication Abstract from PubMedThe structure of death receptor 4 (DR4) in complex with TNF-related apoptosis-inducing ligand (TRAIL) has been determined at 3 A 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. The structure of the death receptor 4-TNF-related apoptosis-inducing ligand (DR4-TRAIL) complex.,Ramamurthy V, Yamniuk AP, Lawrence EJ, Yong W, Schneeweis LA, Cheng L, Murdock M, Corbett MJ, Doyle ML, Sheriff S Acta Crystallogr F Struct Biol Commun. 2015 Oct;71(Pt 10):1273-81. doi:, 10.1107/S2053230X15016416. Epub 2015 Sep 23. PMID:26457518[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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