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

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 h...

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Bibliographic Details
Published in:Molecular cell 2003-04, Vol.11 (4), p.965-976
Main Authors: Selenko, Philipp, Gregorovic, Goran, Sprangers, Remco, Stier, Gunter, Rhani, Zakaria, Krämer, Angela, Sattler, Michael
Format: Article
Language:English
Subjects:
Amino Acid Sequence - genetics
Binding Sites - genetics
DNA Mutational Analysis
DNA-Binding Proteins
Humans
Molecular Conformation
Molecular Structure
Nuclear Proteins
Protein Structure, Secondary - genetics
Protein Structure, Tertiary - genetics
Ribonucleoproteins - genetics
Ribonucleoproteins - metabolism
RNA Splice Sites - genetics
RNA Splicing - genetics
RNA Splicing Factors
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
Sequence Homology, Amino Acid
Splicing Factor U2AF
Transcription Factors
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Summary: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.
ISSN:1097-2765
DOI:10.1016/s1097-2765(03)00115-1