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PDBsum entry 2mtf
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RNA binding protein
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PDB id
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2mtf
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References listed in PDB file
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Key reference
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Title
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Synergic interplay of the la motif, Rrm1 and the interdomain linker of larp6 in the recognition of collagen mRNA expands the RNA binding repertoire of the la module.
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Authors
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L.Martino,
S.Pennell,
G.Kelly,
B.Busi,
P.Brown,
R.A.Atkinson,
N.J.Salisbury,
Z.H.Ooi,
K.W.See,
S.J.Smerdon,
C.Alfano,
T.T.Bui,
M.R.Conte.
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Ref.
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Nucleic Acids Res, 2015,
43,
645-660.
[DOI no: ]
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PubMed id
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Abstract
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The La-related proteins (LARPs) form a diverse group of RNA-binding proteins
characterized by the possession of a composite RNA binding unit, the La module.
The La module comprises two domains, the La motif (LaM) and the RRM1, which
together recognize and bind to a wide array of RNA substrates. Structural
information regarding the La module is at present restricted to the prototypic
La protein, which acts as an RNA chaperone binding to 3' UUUOH sequences of
nascent RNA polymerase III transcripts. In contrast, LARP6 is implicated in the
regulation of collagen synthesis and interacts with a specific stem-loop within
the 5' UTR of the collagen mRNA. Here, we present the structure of the LaM and
RRM1 of human LARP6 uncovering in both cases considerable structural variation
in comparison to the equivalent domains in La and revealing an unprecedented
fold for the RRM1. A mutagenic study guided by the structures revealed that RNA
recognition requires synergy between the LaM and RRM1 as well as the
participation of the interdomain linker, probably in realizing tandem domain
configurations and dynamics required for substrate selectivity. Our study
highlights a considerable complexity and plasticity in the architecture of the
La module within LARPs.
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Secondary reference #1
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Title
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1h, 15n and 13c chemical shift assignments of the la and rrm1 from human larp6
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Authors
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L.Martino,
S.Pennell,
G.Kelly,
B.Busi,
P.Brown,
A.R.Atkinsn.Jh.Salisbury,
Z.H.Ooi,
K.W.See,
S.J.Smerdon,
C.Alfano,
T.Tt.Bui,
M.R.Conte.
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Ref.
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TO BE PUBLISHED ...
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