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

Mol Cell. 2003 Apr;11(4):965-76. doi: 10.1016/s1097-2765(03)00115-1.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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 Splicing Factors
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism*
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*
  • Ribonucleoproteins / genetics
  • Ribonucleoproteins / metabolism*
  • Sequence Homology, Amino Acid
  • Splicing Factor U2AF
  • Transcription Factors*

Substances

  • DNA-Binding Proteins
  • Nuclear Proteins
  • RNA Splice Sites
  • RNA Splicing Factors
  • RNA, Messenger
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • SF1 protein, human
  • Splicing Factor U2AF
  • Transcription Factors
  • U2AF2 protein, human

Associated data

  • PDB/1O0P