Premium
Structural and functional study of FK domain of Fstl1
Author(s) -
Li Xinxin,
Li Lian,
Chang Yue,
Ning Wen,
Liu Xinqi
Publication year - 2019
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3696
Subject(s) - dimer , function (biology) , domain (mathematical analysis) , chemistry , molecule , signal transduction , microbiology and biotechnology , biophysics , computational biology , biology , biochemistry , mathematics , mathematical analysis , organic chemistry
Fstl1 is a TGF‐β 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‐β, 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‐β signaling. These observations provide important insights into the understanding of Fstl1 and may facilitate the exploration of this molecule in clinical study.