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Scientific article
English

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

Contributors

Selenko, Philipp; Gregorovic, Goran; Sprangers, Remco; Stier, Gunter; Rhani, Zakaria; Kraemer, Angela; Sattler, Michael

Published in

Molecular cell, vol. 11, no. 4, p. 965-976

Publication date

2003

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/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

Note

Collboration between Krämer and Sattler groups

UNIGE affiliation entities

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

Identifiers

Additional URL for this publication

http://preview.ncbi.nlm.nih.gov/pubmed/12718882

Journal ISSN

1097-2765
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Technical informations

Creation

22/11/2011 14:48:00

First validation

22/11/2011 14:48:00

Update

14/03/2023 17:04:42

Status update

14/03/2023 17:04:42

Last indexation

29/10/2024 18:37:49
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