Structure of TRAF Family: Current Understanding of Receptor Recognition.

Structure of TRAF Family: Current Understanding of Receptor Recognition.
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DOI:
10.3389/fimmu.2018.01999
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发表时间:
2018
影响因子:
7.3
通讯作者:
Park HH
Park HH
中科院分区:
医学2区
文献类型:
--
作者:
Park HH

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肿瘤坏死因子受体相关因子(TRAF)蛋白是在包括免疫应答、细胞死亡和存活、发育和血栓形成的各种细胞信号传导事件中起作用的关键信号传导分子。它们在细胞信号传导中的作用主要通过TRAF结构域与各种受体的直接相互作用来介导。为了确定特定TRAF结构域如何与具有有限结合界面的各种受体相互作用以及TRAF家族成员的类似结合界面如何识别其特异性结合伴侣,对TRAF家族蛋白的广泛结构研究已经进行了几十年。在这篇综述中,我们讨论了目前的理解的TRAF结构域和TRAF结合基序在许多受体的结构和分子多样性,根据现有的结构信息。
Tumor necrosis factor receptor–associated factor (TRAF) proteins are key signaling molecules that function in various cellular signaling events including immune response, cell death and survival, development, and thrombosis. Their roles in cellular signaling are mediated mostly by direct interactions with various receptors via the TRAF domain. To determine how specific TRAF domains can interact with various receptors with a limited binding interface and how similar binding interfaces of TRAF family members can recognize their specific binding partners, extensive structural studies on TRAF family proteins have been conducted for several decades. In this review, we discuss the current understanding of the structural and molecular diversity of the TRAF domain and TRAF-binding motifs in many receptors according to available structural information.
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