Specificity of molecular recognition learned from the crystal structures of TRAIL and the TRAIL:sDR5 complex.
TRAIL is a member of the tumor necrosis factor (TNF) superfamily. TRAIL has drawn a lasting attention because of its selectivity and efficacy in inducing apoptosis in a variety of cancer cells but not in normal cells. The structures of both TRAIL and the protein in complex with the extracellular domain of death receptor 5 (sDR5) were elucidated. Because each factor of the ligand family and the receptor family is large, it poses an intriguing question of how recognition between cognate ligands and receptors is achieved in a highly specific manner without cross interactions. This review focuses on the unique properties of TRAIL and molecular strategies for the specific recognition between the two family members primarily based on the crystal structures of TRAIL and the TRAIL:sDR5 complex.
Cha
Sun-Shin
SS
Beamline Division, Pohang Accelerator Laboratory, Korea.
Song
Young-Lan
YL
Oh
Byung-Ha
BH
D000595:Amino Acid Sequence; D000818:Animals; D051017:Apoptosis Regulatory Proteins; D001665:Binding Sites; D003460:Crystallization; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017433:Protein Structure, Secondary; D053220:Receptors, TNF-Related Apoptosis-Inducing Ligand; D018124:Receptors, Tumor Necrosis Factor / Q000737:chemistry* / Q000378:metabolism*; D053221:TNF-Related Apoptosis-Inducing Ligand; D014409:Tumor Necrosis Factor-alpha / Q000737:chemistry* / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism
D051017:Apoptosis Regulatory Proteins; D008562:Membrane Glycoproteins; D053220:Receptors, TNF-Related Apoptosis-Inducing Ligand; D018124:Receptors, Tumor Necrosis Factor; D053221:TNF-Related Apoptosis-Inducing Ligand; C505639:TNFRSF10B protein, human; C505653:TNFSF10 protein, human; D014409:Tumor Necrosis Factor-alpha; D015032:Zinc