2.8 angstrom resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity

TRAIL is a newly identified cytokine belonging to the large tumor necrosis factor (TNF) family. TRAIL is a novel molecule inducing apoptosis in a wide variety of tumor cells but not in normal cells. To help in elucidating its biological roles and designing mutants with improved therapeutic potential, we have determined the crystal structure of human TRAIL. The structure reveals that a unique frame insertion of 12-16 amino acids adopts a salient loop structure penetrating into the receptor-binding site. The loop drastically alters the common receptor-binding surface of the TNF family most likely for the specific recognition of cognate partners. A structure-based mutagenesis study demonstrates a critical role of the insertion loop in the cytotoxic activity of TRAIL.
Publisher
CELL PRESS
Issue Date
1999-08
Language
ENG
Keywords

TUMOR-NECROSIS-FACTOR; TNF RECEPTOR SUPERFAMILY; FACTOR-ALPHA; LIGAND TRAIL; FAMILY; APOPTOSIS; DEATH; ACTIVATION; OSTEOPROTEGERIN; DOMAIN

Citation

IMMUNITY, v.11, no.2, pp.253 - 261

ISSN
1074-7613
DOI
10.1016/S1074-7613(00)80100-4
URI
http://hdl.handle.net/10203/74727
Appears in Collection
BS-Journal Papers(저널논문)
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