1o0p

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==Overview==
==Overview==
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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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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==
==About this Structure==
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[[Category: non-canonical rna recognition motif]]
[[Category: non-canonical rna recognition motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:31:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:12:15 2008''

Revision as of 12:12, 21 February 2008


1o0p

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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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