Crystal structure of human YTHDC2 YTH domain

N6-methyladenosine (m6A) readers play an important role in mRNA functions and metabolism. YTHDC2, as one of the m6A readers, controls fertileness through decreasing associated mRNA abundance and enhancing the translation efficiency of related mRNA via binding the targeted m6A RNA. However, how YTH domain of YTHDC2 recognize m6A 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 m6A binding pocket, and similar RNA binding surface shared by YTHDC1.