Summary information and primary citation
- PDB-id
-
1b7f;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- RNA-binding protein-RNA
- Method
- X-ray (2.6 Å)
- Summary
- Sxl-lethal protein-RNA complex
- Reference
-
Handa N, Nureki O, Kurimoto K, Kim I, Sakamoto H, Shimura
Y, Muto Y, Yokoyama S (1999): "Structural
basis for recognition of the tra mRNA precursor by the
Sex-lethal protein." Nature,
398, 579-585. doi: 10.1038/19242.
- Abstract
- The Sex-lethal (Sxl) protein of Drosophila melanogaster
regulates alternative splicing of the transformer (tra)
messenger RNA precursor by binding to the tra
polypyrimidine tract during the sex-determination process.
The crystal structure has now been determined at 2.6 A
resolution of the complex formed between two tandemly
arranged RNA-binding domains of the Sxl protein and a
12-nucleotide, single-stranded RNA derived from the tra
polypyrimidine tract. The two RNA-binding domains have
their beta-sheet platforms facing each other to form a
V-shaped cleft. The RNA is characteristically extended and
bound in this cleft, where the UGUUUUUUU sequence is
specifically recognized by the protein. This structure
offers the first insight, to our knowledge, into how a
protein binds specifically to a cognate RNA without any
intramolecular base-pairing.