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1o0p
From Proteopedia
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'''Solution Structure of the third RNA Recognition Motif (RRM) of U2AF65 in complex with an N-terminal SF1 peptide''' | '''Solution Structure of the third RNA Recognition Motif (RRM) of U2AF65 in complex with an N-terminal SF1 peptide''' | ||
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[[Category: 2 alpha helices additionally extended by a third helix c]] | [[Category: 2 alpha helices additionally extended by a third helix c]] | ||
[[Category: 4-stranded anti-parallel beta-sheet]] | [[Category: 4-stranded anti-parallel beta-sheet]] | ||
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Revision as of 00:13, 3 May 2008
Solution Structure of the third RNA Recognition Motif (RRM) of U2AF65 in complex with an N-terminal SF1 peptide
Overview
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.
About this Structure
1O0P is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP., Selenko P, Gregorovic G, Sprangers R, Stier G, Rhani Z, Kramer A, Sattler M, Mol Cell. 2003 Apr;11(4):965-76. PMID:12718882 Page seeded by OCA on Sat May 3 03:13:02 2008
