2MTV

Solution Structure of the YTH Domain of YT521-B in complex with N6-Methyladenosine containing RNA

Summary for 2MTV

• Entry DOI: 10.2210/pdb2mtv/pdb
• NMR Information: BMRB: 25188
• Descriptor: YTH domain-containing protein 1, RNA_(5'-R(*UP*GP*(6MZ)P*CP*AP*C)-3') (2 entities in total)
• Functional Keywords: yth, m6a, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Rattus norvegicus (brown rat,rat,rats); More
• Cellular location: Nucleus : Q9QY02
• Total number of polymer chains: 2
• Total formula weight: 19397.41

Authors

Theler, D.,Dominguez, C.,Blatter, M.,Boudet, J.,Allain, F.H.-T. (deposition date: 2014-09-01, release date: 2014-11-26, Last modification date: 2024-05-01)

Primary citation

Theler, D.,Dominguez, C.,Blatter, M.,Boudet, J.,Allain, F.H.
Solution structure of the YTH domain in complex with N6-methyladenosine RNA: a reader of methylated RNA.
Nucleic Acids Res., 42:13911-13919, 2014

PubMed Abstract: N(6)A methylation is the most abundant RNA modification occurring within messenger RNA. Impairment of methylase or demethylase functions are associated with severe phenotypes and diseases in several organisms. Beside writer and eraser enzymes of this dynamic RNA epigenetic modification, reader proteins that recognize this modification are involved in numerous cellular processes. Although the precise characterization of these reader proteins remains unknown, preliminary data showed that most potential reader proteins contained a conserved YT521-B homology (YTH) domain. Here we define the YTH domain of rat YT521-B as a N(6)-methylated adenosine reader domain and report its solution structure in complex with a N(6)-methylated RNA. The structure reveals a binding preference for NGANNN RNA hexamer and a deep hydrophobic cleft for m(6)A recognition. These findings establish a molecular function for YTH domains as m(6)A reader domains and should guide further studies into the biological functions of YTH-containing proteins in m(6)A recognition.

PubMed: 25389274
DOI: 10.1093/nar/gku1116

Experimental method

SOLUTION NMR