1o0p
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(New page: 200px<br /> <applet load="1o0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o0p" /> '''Solution Structure of the third RNA Recogni...)
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Revision as of 16:21, 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
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
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