Structural Basis for the Molecular Recognition between Human Splicing Factors U2AF 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 super(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively cha...

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Bibliographic Details
Published in:Molecular cell 2003-04, Vol.11 (4), p.965-976
Main Authors: Selenko, P, Gregorovic, G, Sprangers, R, Stier, G, Rhani, Z, Kraemer, A, Sattler, M
Format: Article
Language:English
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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 super(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