运输机
同源(生物学)
生物
超家族
转运蛋白
生物化学
脂蛋白
ATP结合盒运输机
膜蛋白
蛋白质超家族
激活剂(遗传学)
溶质载体族
脂滴
细胞生物学
功能(生物学)
基因
膜
胆固醇
作者
Yong Wei,Zi Jian Xiong,Jun Li,Chunxia Zou,Christopher W. Cairo,John S. Klassen,Gilbert G. Privé
标识
DOI:10.1038/s42003-018-0262-9
摘要
Abstract EPDR1, a member of the ependymin-related protein family, is a relatively uncharacterized protein found in the lysosomes and secretomes of most vertebrates. Despite having roles in human disease and health, the molecular functions of EPDR1 remain unknown. Here, we present crystal structures of human EPDR1 and reveal that the protein adopts a fold previously seen only in bacterial proteins related to the LolA lipoprotein transporter. EPDR1 forms a homodimer with an overall shape resembling a half-shell with two non-overlapping hydrophobic grooves on the flat side of the hemisphere. EPDR1 can interact with membranes that contain negatively charged lipids, including BMP and GM1, and we suggest that EPDR1 may function as a lysosomal activator protein or a lipid transporter. A phylogenetic analysis reveals that the fold is more widely distributed than previously suspected, with representatives identified in all branches of cellular life.
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