Crystal structure of human YTHDC2 YTH domain

被引:29
作者
Ma, Chao [1 ,2 ]
Liao, Shanhui [1 ,2 ]
Zhu, Zhongliang [1 ,2 ]
机构
[1] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230027, Peoples R China
[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230027, Peoples R China
关键词
Crystal structure; YTHDC2; YTH domain; m(6)A RNA; NUCLEAR-RNA; M(6)A RNA; PROTEIN; BINDING; RECOGNITION; TRANSLATION; METABOLISM; REVEALS; COMPLEX; TOOLS;
D O I
10.1016/j.bbrc.2019.08.107
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
N-6-methyladenosine (m(6)A) "readers" play an important role in mRNA functions and metabolism. YTHDC2, as one of the m(6)A readers, controls fertileness through decreasing associated mRNA abundance and enhancing the translation efficiency of related mRNA via binding the targeted m(6)A RNA. However, how YTH domain of YTHDC2 recognize m(6)A RNA is still unknown. In this study, we determined the crystal structure of human YTHDC2 YTH domain, which adopts similar architecture to other solved YTH domain structures. YTHDC2 contains a conserved m(6)A binding pocket, and similar RNA binding surface shared by YTHDCI. (C) 2019 Elsevier Inc. All rights reserved.
引用
收藏
页码:678 / 684
页数:7
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