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PDBsum entry 4r3h

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protein ligands Protein-protein interface(s) links
RNA binding protein PDB id
4r3h

 

 

 

 

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Contents
Protein chains
157 a.a.
Ligands
UNX ×11
SO4
Waters ×158
PDB id:
4r3h
Name: RNA binding protein
Title: The crystal structure of an apo RNA binding protein
Structure: Yth domain-containing protein 1. Chain: a, b. Synonym: putative splicing factor yt521, yt521-b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ythdc1, kiaa1966, yt521. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.193     R-free:   0.240
Authors: C.Xu,K.Liu,W.Tempel,Y.Li,C.Bountra,C.H.Arrowsmith,A.M.Edwards,J.Min, Structural Genomics Consortium (Sgc)
Key ref: C.Xu et al. (2014). Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain. Nat Chem Biol, 10, 927-929. PubMed id: 25242552 DOI: 10.1038/nchembio.1654
Date:
15-Aug-14     Release date:   17-Sep-14    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q96MU7  (YTDC1_HUMAN) -  YTH domain-containing protein 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
727 a.a.
157 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1038/nchembio.1654 Nat Chem Biol 10:927-929 (2014)
PubMed id: 25242552  
 
 
Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain.
C.Xu, X.Wang, K.Liu, I.A.Roundtree, W.Tempel, Y.Li, Z.Lu, C.He, J.Min.
 
  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.
 

 

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