Structural basis for the molecular recognition bet...[Mol Cell. 2003]

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1: Mol Cell. 2003 Apr;11(4):965-76. Links

Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP.

Selenko P, Gregorovic G, Sprangers R, Stier G, Rhani Z, Krämer A, Sattler M.

European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.

The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.

PMID: 12718882 [PubMed - indexed for MEDLINE]

The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF 65) is essential in vivo but dispensable for activity in vitro.
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[Mol Cell Biol. 2001]
Conservation of functional domains involved in RNA binding and protein-protein interactions in human and Saccharomyces cerevisiae pre-mRNA splicing factor SF1.
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[RNA. 1998]
ReviewU2AF homology motifs: protein recognition in the RRM world.
Genes Dev. 2004 Jul 1; 18(13):1513-26.

[Genes Dev. 2004]
ReviewBroad specificity of SR (serine/arginine) proteins in the regulation of alternative splicing of pre-messenger RNA.
Prog Nucleic Acid Res Mol Biol. 2004; 78:37-88.

[Prog Nucleic Acid Res Mol Biol. 2004]
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Cited by 19 PubMed Central articles

The RRM domain in GW182 proteins contributes to miRNA-mediated gene silencing.
Eulalio A, Tritschler F, Büttner R, Weichenrieder O, Izaurralde E, Truffault V. Nucleic Acids Res. 2009 May; 37(9):2974-83. Epub 2009 Mar 18.

[Nucleic Acids Res. 2009]
Structure of the yeast Pml1 splicing factor and its integration into the RES complex.
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[Nucleic Acids Res. 2009]
Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65.
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[Mol Biol Cell. 2008]
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Structures reported by this article

Solution Structure Of The Third Rna Recognition Motif (Rrm) Of U2af65 In Complex With An N-Terminal Sf1 Peptide

PDB: 1OPI

Source: Homo sapiens

Method: Nmr, 10 Structures
» See all 2 structures...

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Cited by 19 PubMed Central articles

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