Scientific article

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

Published inMolecular cell, vol. 11, no. 4, p. 965-976
Publication date2003

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.

  • 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
  • RNA Splice Sites/genetics
  • RNA Splicing/genetics
  • RNA, Messenger/genetics/metabolism
  • RNA-Binding Proteins/genetics/metabolism
  • Ribonucleoproteins/genetics/metabolism
  • Sequence Homology, Amino Acid
  • Transcription Factors
NoteCollboration between Krämer and Sattler groups
Citation (ISO format)
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. 965–976. doi: 10.1016/S1097-2765(03)00115-1
ISSN of the journal1097-2765

Technical informations

Creation11/22/2011 2:48:00 PM
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