UNIGE document Scientific Article
previous document  unige:17544  next document
add to browser collection
Title

Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
Authors
Selenko, Philipp
Gregorovic, Goran
Sprangers, Remco
Stier, Gunter
Rhani, Zakaria
Kraemer, Angela
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/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
Identifiers
PMID: 12718882
Note Collboration between Krämer and Sattler groups
Full text
Other version: http://preview.ncbi.nlm.nih.gov/pubmed/12718882
Structures
Faculté des sciences / Section de biologie / Département de biologie cellulaire
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. 965-76. https://archive-ouverte.unige.ch/unige:17544

149 hits

0 download

Contact an author

Update request

Update

Deposited on : 2011-11-25

Export document
Format :
Citation style :