Abstract:
: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.
journal_name
Immunityjournal_title
Immunityauthors
Cha SS,Kim MS,Choi YH,Sung BJ,Shin NK,Shin HC,Sung YC,Oh BHdoi
10.1016/s1074-7613(00)80100-4keywords:
subject
Has Abstractpub_date
1999-08-01 00:00:00pages
253-61issue
2eissn
1074-7613issn
1097-4180pii
S1074-7613(00)80100-4journal_volume
11pub_type
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