Specificity of Molecular Recognition Learned from the Crystal Structures of TRAIL and the TRAIL:sDR5 Complex

Sun Shin Cha; Young Lan Song; Byung Ha Oh

doi:10.1016/S0083-6729(04)67001-4

Specificity of Molecular Recognition Learned from the Crystal Structures of TRAIL and the TRAIL:sDR5 Complex

Sun Shin Cha, Young Lan Song, Byung Ha Oh

Department of Chemistry & Nanoscience

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

3 Scopus citations

Abstract

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.

Original language	English
Title of host publication	TRAIL (TNF-Related Apoptosis-Inducing Ligand)
Publisher	Academic Press Inc.
Pages	1-17
Number of pages	17
ISBN (Print)	0127098674, 9780127098678
DOIs	https://doi.org/10.1016/S0083-6729(04)67001-4
State	Published - 2004

Publication series

Name	Vitamins and Hormones
Volume	67
ISSN (Print)	0083-6729

Bibliographical note

Funding Information:
Supported by Creative Research Initiatives of the Korean Ministry of Science and Technology.

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10.1016/S0083-6729(04)67001-4

Cite this

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abstract = "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.",

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AU - Song, Young Lan

AU - Oh, Byung Ha

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AB - 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.

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DO - 10.1016/S0083-6729(04)67001-4

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AN - SCOPUS:3042779891

SN - 0127098674

SN - 9780127098678

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BT - TRAIL (TNF-Related Apoptosis-Inducing Ligand)

PB - Academic Press Inc.

ER -

Specificity of Molecular Recognition Learned from the Crystal Structures of TRAIL and the TRAIL:sDR5 Complex

Abstract

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