1opi
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(New page: 200px<br /> <applet load="1opi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1opi" /> '''SOLUTION STRUCTURE OF THE THIRD RNA RECOGNI...)
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Revision as of 16:28, 12 November 2007
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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
1OPI 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
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