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PDBsum entry 2rok
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RNA binding protein
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PDB id
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2rok
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References listed in PDB file
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Key reference
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Title
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The rrm domain of poly(a)-Specific ribonuclease has a noncanonical binding site for mRNA cap analog recognition.
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Authors
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T.Nagata,
S.Suzuki,
R.Endo,
M.Shirouzu,
T.Terada,
M.Inoue,
T.Kigawa,
N.Kobayashi,
P.Güntert,
A.Tanaka,
Y.Hayashizaki,
Y.Muto,
S.Yokoyama.
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Ref.
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Nucleic Acids Res, 2008,
36,
4754-4767.
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PubMed id
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Abstract
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The degradation of the poly(A) tail is crucial for posttranscriptional gene
regulation and for quality control of mRNA. Poly(A)-specific ribonuclease (PARN)
is one of the major mammalian 3' specific exo-ribonucleases involved in the
degradation of the mRNA poly(A) tail, and it is also involved in the regulation
of translation in early embryonic development. The interaction between PARN and
the m(7)GpppG cap of mRNA plays a key role in stimulating the rate of
deadenylation. Here we report the solution structures of the cap-binding domain
of mouse PARN with and without the m(7)GpppG cap analog. The structure of the
cap-binding domain adopts the RNA recognition motif (RRM) with a characteristic
alpha-helical extension at its C-terminus, which covers the beta-sheet surface
(hereafter referred to as PARN RRM). In the complex structure of PARN RRM with
the cap analog, the base of the N(7)-methyl guanosine (m(7)G) of the cap analog
stacks with the solvent-exposed aromatic side chain of the distinctive
tryptophan residue 468, located at the C-terminal end of the second beta-strand.
These unique structural features in PARN RRM reveal a novel cap-binding mode,
which is distinct from the nucleotide recognition mode of the canonical RRM
domains.
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