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

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

Immunity

journal_title

Immunity

authors

Cha SS,Kim MS,Choi YH,Sung BJ,Shin NK,Shin HC,Sung YC,Oh BH

doi

10.1016/s1074-7613(00)80100-4

keywords:

subject

Has Abstract

pub_date

1999-08-01 00:00:00

pages

253-61

issue

2

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(00)80100-4

journal_volume

11

pub_type

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