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

Selenko, Philipp
Sprangers, Remco
Stier, Gunter
Sattler, Michael
Published in Molecular cell. 2003, vol. 11, no. 4, p. 965-76
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.
Keywords Amino Acid Sequence/geneticsBinding Sites/geneticsDNA Mutational AnalysisDNA-Binding ProteinsHumansMolecular ConformationMolecular StructureNuclear ProteinsProtein Structure, Secondary/geneticsProtein Structure, Tertiary/geneticsRNA Splice Sites/geneticsRNA Splicing/geneticsRNA, Messenger/genetics/metabolismRNA-Binding Proteins/genetics/metabolismRibonucleoproteins/genetics/metabolismSequence Homology, Amino AcidTranscription Factors
PMID: 12718882
Note Collboration between Krämer and Sattler groups
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SELENKO, Philipp et al. Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP. In: Molecular cell, 2003, vol. 11, n° 4, p. 965-76. doi: 10.1016/S1097-2765(03)00115-1 https://archive-ouverte.unige.ch/unige:17544

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Deposited on : 2011-11-25

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