1O0P: Solution Structure of the third RNA Recognition Motif (RRM) of U2AF65 in complex with an N-terminal SF1 peptide

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.
PDB ID: 1O0PDownload
MMDB ID: 22760
PDB Deposition Date: 2003/2/24
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Homo sapiens
Similar Structures:
Molecular Components in 1O0P
Label Count Molecule
Proteins (2 molecules)
Splicing Factor U2af 65 KDA Subunit(Gene symbol: U2AF2)
Molecule annotation
Splicing Factor SF1(Gene symbol: SF1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB