1o0p
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0p OCA], [http://www.ebi.ac.uk/pdbsum/1o0p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o0p RCSB]</span> | ||
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[[Category: non-canonical rna recognition motif]] | [[Category: non-canonical rna recognition motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:38:09 2008'' |
Revision as of 19:38, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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