Structural basis for the interaction of TAK1 kinase with its activating protein TAB1

被引：82

作者：

Brown, K ^{[1
]}

Vial, SCM ^{[1
]}

Dedi, N ^{[1
]}

Long, JM ^{[1
]}

Dunster, NJ ^{[1
]}

Cheetham, GMT ^{[1
]}

机构：

[1] Vertex Pharmaceut Europe Ltd, Abingdon OX14 4RY, Oxon, England

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2005年 / 354卷 / 05期

关键词：

TAK1; TAB1; kinase; inflammation; apoptosis;

D O I：

10.1016/j.jmb.2005.09.098

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Transforming growth factor-P (TGF-beta)-activated kinase 1 (TAK1) is a member of the MAPKKK family of protein kinases, and is involved in intracellular signalling pathways stimulated by transforming growth factor beta, interleukin-1 and tumour necrosis factor-alpha. TAK1 is known to rely upon an additional protein, TAK1-binding protein 1 (TAB1), for complete activation. However, the molecular basis for this activation has yet to be elucidated. We have solved the crystal structure of a novel TAKI chimeric protein and these data give insight into how TAK1 is activated by TAB1. Our results reveal a novel binding pocket on the TAK1 kinase domain whose shape complements that of a unique alpha-helix in the TAK1 binding domain of TAB1, providing the basis for an intimate hydrophobic association between the protein activator and its target. (c) 2005 Elsevier Ltd. All rights reserved.

引用

页码：1013 / 1020

页数：8

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