FYCO1 RUN 结构域的晶体结构表明其可能与小 GTPases 相互作用。
Crystal structure of the FYCO1 RUN domain suggests possible interfaces with small GTPases.
机构信息
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
出版信息
Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):326-333. doi: 10.1107/S2053230X20009012. Epub 2020 Jul 28.
Abstract
FYCO1 is a multidomain adaptor protein that plays an important role in autophagy by mediating the kinesin-dependent microtubule plus-end-directed transport of autophagosomes. FYCO1 contains a RUN domain, which is hypothesized to function as a specific effector for members of the Ras superfamily of small GTPases, but its role has not been well characterized and its interaction partner(s) have not been identified. Here, the crystal structure of the FYCO1 RUN domain was determined at 1.3 Å resolution. The overall structure of the FYCO1 RUN domain was similar to those of previously reported RUN domains. Detailed structural comparisons with other RUN domains and docking studies suggested a possible interaction interface of the FYCO1 RUN domain with small GTPases of the Ras superfamily.
摘要
FYCO1 是一种多结构域衔接蛋白，通过介导动力蛋白依赖的微管正极端指向的自噬体运输，在自噬中发挥重要作用。FYCO1 含有一个 RUN 结构域，该结构域被假设为 Ras 超家族小分子 GTP 酶成员的特异性效应因子，但它的作用尚未得到很好的描述，其相互作用伙伴也尚未确定。在这里，FYCO1 RUN 结构域的晶体结构在 1.3Å 分辨率下被确定。FYCO1 RUN 结构域的整体结构与先前报道的 RUN 结构域相似。与其他 RUN 结构域的详细结构比较和对接研究表明，FYCO1 RUN 结构域与 Ras 超家族的小分子 GTP 酶可能存在相互作用界面。
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