SGD Paper 
Ohi MD, et al. (2003) Structural insights into the U-box, a domain associated with multi-ubiquitination. Nat Struct Biol 10(4):250-5
Abstract: The structure of the U-box in the essential Saccharomyces cerevisiae pre-mRNA splicing factor Prp19p has been determined by NMR. The conserved zinc-binding sites supporting the cross-brace arrangement in RING-finger domains are replaced by hydrogen-bonding networks in the U-box. These hydrogen-bonding networks are necessary for the structural stabilization and activity of the U-box. A conservative Val-->Ile point mutation in the Prp19p U-box domain leads to pre-mRNA splicing defects in vivo. NMR analysis of this mutant shows that the substitution disrupts structural integrity of the U-box domain. Furthermore, comparison of the Prp19p U-box domain with known RING-E2 complex structures demonstrates that both U-box and RING-fingers contain a conserved interaction surface. Mutagenesis of residues at this interface, while not perturbing the structure of the U-box, abrogates Prp19p function in vivo. These comparative structural and functional analyses imply that the U-box and its associated ubiquitin ligase activity are critical for Prp19p function in vivo.
| Status: Published | Type: Journal Article | PubMed ID: 12627222 |
Topics addressed in this paper
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| Topics | Genes linked to topics |
|---|---|
| PRP19 | |
| Function/Process |  |
| Mutants/Phenotypes | |
| Primary Literature | |
| Protein Sequence Features | |
| Protein/Nucleic Acid Structure | |
| Strains/Constructs | |
