1OPI

SOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2AF65 IN COMPLEX WITH AN N-TERMINAL SF1 PEPTIDE

Summary for 1OPI

• Entry DOI: 10.2210/pdb1opi/pdb
• Related: 1O0P
• Descriptor: SPLICING FACTOR U2AF 65 KDA SUBUNIT, SPLICING FACTOR SF1 (2 entities in total)
• Functional Keywords: non-canonical rna recognition motif, 4-stranded anti-parallel beta-sheet, 2 alpha helices additionally extended by a third helix c, rna binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P26368 Q15637
• Total number of polymer chains: 2
• Total formula weight: 13668.55

Authors

Selenko, P.,Gregorovic, G.,Sprangers, R.,Stier, G.,Rhani, Z.,Kramer, A.,Sattler, M. (deposition date: 2003-03-05, release date: 2004-03-16, Last modification date: 2024-05-22)

Primary citation

Selenko, P.,Gregorovic, G.,Sprangers, R.,Stier, G.,Rhani, Z.,Kramer, A.,Sattler, M.
Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
Mol.Cell, 11:965-976, 2003

PubMed Abstract: 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.

PubMed: 12718882
DOI: 10.1016/S1097-2765(03)00115-1

Experimental method

SOLUTION NMR