This work describes structural and biochemical investigations of cooperative recognition of 3’ splice site by splicing factor 1 (SF1) and large subunit (U2AF65) of the U2 snRNP auxiliary factor. The structure of the N-terminal domain of SF1 was determined by NMR, the influences of the phosphorylation of two serine residues on the conformation and interactions were investigated. This study provides novel insights into molecular mechanisms of recognition of 3’ splice site and the regulation of splicing.
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This work describes structural and biochemical investigations of cooperative recognition of 3’ splice site by splicing factor 1 (SF1) and large subunit (U2AF65) of the U2 snRNP auxiliary factor. The structure of the N-terminal domain of SF1 was determined by NMR, the influences of the phosphorylation of two serine residues on the conformation and interactions were investigated. This study provides novel insights into molecular mechanisms of recognition of 3’ splice site and the regulation of spl...
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