FADD死亡结构域的溶液结构。Fas和FADD死亡结构域相互作用的结构基础。

The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.

作者信息

Jeong E J, Bang S, Lee T H, Park Y I, Sim W S, Kim K S

机构信息

Structural Biology Center, Korea Institute of Science and Technology, Seoul, 130-650, Korea University, Seoul, 136-701, Korea.

出版信息

J Biol Chem. 1999 Jun 4;274(23):16337-42. doi: 10.1074/jbc.274.23.16337.

DOI:10.1074/jbc.274.23.16337

PMID:10347191

Abstract

A signal of Fas-mediated apoptosis is transferred through an adaptor protein Fas-associated death domain protein (FADD) by interactions between the death domains of Fas and FADD. To understand the signal transduction mechanism of Fas-mediated apoptosis, we solved the solution structure of a murine FADD death domain. It consists of six helices arranged in a similar fold to the other death domains. The interactions between the death domains of Fas and FADD analyzed by site-directed mutagenesis indicate that charged residues in helices alpha2 and alpha3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, alpha2 of FADD with alpha3 of Fas and vice versa.

摘要

Fas介导的凋亡信号通过衔接蛋白Fas相关死亡结构域蛋白（FADD）传递，这是由Fas和FADD的死亡结构域之间的相互作用实现的。为了理解Fas介导的凋亡信号转导机制，我们解析了小鼠FADD死亡结构域的溶液结构。它由六个螺旋组成，其折叠方式与其他死亡结构域相似。通过定点诱变分析Fas和FADD的死亡结构域之间的相互作用表明，α2和α3螺旋中的带电荷残基参与死亡结构域相互作用，并且相互作用的螺旋似乎以反平行模式相互作用，FADD的α2与Fas的α3相互作用，反之亦然。