Structural and functional study of FK domain of Fstl1
Structural and functional study of FK domain of Fstl1
复制标题
Fstl1 FK结构域的结构和功能研究
DOI：
10.1002/pro.3696
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发表时间：
2019-08-09
期刊：
影响因子：
8
通讯作者：
Liu, Xinqi
中科院分区：
文献类型：
--
作者：
Li, Xinxin;Li, Lian;Liu, Xinqi
Fstl1 is a TGF-beta superfamily binding protein which involved in many pathological processes. The function of Fstl1 has been widely elucidated, but its structural characterization has not been explored. Here we solved the high-resolution crystal structure of FK domain of murine Fstl1, analyzed its unique characteristics, and investigated its contribution to the function of full-length Fstl1. We found that Fstl1-FK forms a stable dimer in both solution and crystal, which suggest that this protein may function as a dimer during its interaction with TGF-beta, a molecule known to form dimer during activation process. We also found this FK domain is indispensable for the proper function of Fstl1 during the transduction of TGF-beta signaling. These observations provide important insights into the understanding of Fstl1 and may facilitate the exploration of this molecule in clinical study.
