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

Selenko, P., Gregorovic, G., Sprangers, R., Stier, G., Rhani, Z., Krämer, A., et al. (2003). Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP. Molecular Cell, 11(4), 965-976. doi:10.1016/S1097-2765(03)00115-1.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0000-3D16-4 Version Permalink: https://hdl.handle.net/21.11116/0000-0000-3D17-3
Genre: Journal Article

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MolCell_11_2003_965.pdf (Any fulltext), 961KB
 
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 Creators:
Selenko, P., Author
Gregorovic, G., Author
Sprangers, R., Author
Stier, Gunter1, Author           
Rhani, Z., Author
Krämer, Annegret2, Author           
Sattler, Michael, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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 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.

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Language(s): eng - English
 Dates: 2003-01-222002-10-112003-01-302003-04-24
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S1097-2765(03)00115-1
URI: http://www.ncbi.nlm.nih.gov/pubmed/12718882
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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 11 (4) Sequence Number: - Start / End Page: 965 - 976 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929