Other version: http://preview.ncbi.nlm.nih.gov/pubmed/12718882
Highlights
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Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP |
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Authors | ||
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 | |
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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. doi: 10.1016/S1097-2765(03)00115-1 https://archive-ouverte.unige.ch/unige:17544 |