Structural highlights
Function
YTDC1_HUMAN RNA-binding protein that regulates alternative splice site selection.[1]
Publication Abstract from PubMed
N6-methyladenosine (m6A) 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 m6A-containing RNA. Our structural studies, together with transcriptome-wide identification of YTHDC1-binding sites and biochemical experiments, not only reveal the specific mode of m6A-YTH binding but also explain the preferential recognition of the GG(m6A)C sequences by YTHDC1.
Structural basis for selective binding of mA RNA by the YTHDC1 YTH domain.,Xu C, Wang X, Liu K, Roundtree IA, Tempel W, Li Y, Lu Z, He C, Min J Nat Chem Biol. 2014 Sep 21. doi: 10.1038/nchembio.1654. PMID:25242552[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang Z, Theler D, Kaminska KH, Hiller M, de la Grange P, Pudimat R, Rafalska I, Heinrich B, Bujnicki JM, Allain FH, Stamm S. The YTH domain is a novel RNA binding domain. J Biol Chem. 2010 May 7;285(19):14701-10. doi: 10.1074/jbc.M110.104711. Epub 2010, Feb 18. PMID:20167602 doi:http://dx.doi.org/10.1074/jbc.M110.104711
- ↑ Xu C, Wang X, Liu K, Roundtree IA, Tempel W, Li Y, Lu Z, He C, Min J. Structural basis for selective binding of mA RNA by the YTHDC1 YTH domain. Nat Chem Biol. 2014 Sep 21. doi: 10.1038/nchembio.1654. PMID:25242552 doi:http://dx.doi.org/10.1038/nchembio.1654
