 |
PDBsum entry 4r3h
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
RNA binding protein
|
PDB id
|
|
|
|
4r3h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structural basis for selective binding of m6a RNA by the ythdc1 yth domain.
|
 |
|
Authors
|
 |
C.Xu,
X.Wang,
K.Liu,
I.A.Roundtree,
W.Tempel,
Y.Li,
Z.Lu,
C.He,
J.Min.
|
 |
|
Ref.
|
 |
Nat Chem Biol, 2014,
10,
927-929.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
|
 |
 |
|
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.
|
 |
|
|
|
|
 |