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

Selenko, P.; Gregorovic, G.; Sprangers, R.; Stier, Gunter; Rhani, Z.; Krämer, Annegret; Sattler, Michael

doi:10.1016/S1097-2765(03)00115-1

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

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Stier, Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Krämer, Annegret
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/pii/S1097276503001151/pdfft?md5=a31869280a1b3840be8a3a024c34b75f&pid=1-s2.0-S1097276503001151-main.pdf
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https://doi.org/10.1016/S1097-2765(03)00115-1
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Citation

Selenko, P., Gregorovic, G., Sprangers, R., Stier, G., Rhani, Z., Krämer, A., et al. (2003). Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP. Molecular Cell, 11(4), 965-976. doi:10.1016/S1097-2765(03)00115-1.

Cite as: https://hdl.handle.net/21.11116/0000-0000-3D16-4

Abstract

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.