| Literature DB >> 25242552 |
Chao Xu1, Xiao Wang2, Ke Liu3, Ian A Roundtree4, Wolfram Tempel5, Yanjun Li5, Zhike Lu6, Chuan He6, Jinrong Min7.
Abstract
N(6)-methyladenosine (m(6)A) is the most abundant internal modification of nearly all eukaryotic mRNAs and has recently been reported to be recognized by the YTH domain family proteins. Here we present the crystal structures of the YTH domain of YTHDC1, a member of the YTH domain family, and its complex with an m(6)A-containing RNA. Our structural studies, together with transcriptome-wide identification of YTHDC1-binding sites and biochemical experiments, not only reveal the specific mode of m(6)A-YTH binding but also explain the preferential recognition of the GG(m(6)A)C sequences by YTHDC1.Entities:
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Year: 2014 PMID: 25242552 DOI: 10.1038/nchembio.1654
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040