Molecular basis of Pirh2-mediated p53 ubiquitylation
NATURE STRUCTURAL & MOLECULAR BIOLOGY（2008）
Abstract
Pirh2 is one of several ubiquitin ligases known to modify and negatively regulate p53. Solution studies reveal the structures of the three Pirh2 domains and indicate that the C-terminal domain of Pirh2 interacts with the p53 tetramerization domain. Additional data suggest that Pirh2 preferentially modifies the tetrameric, transcriptionally active form of p53 for proteasome-mediated degradation.
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Key words
amino acid sequence,biochemistry,genetics,cell biology,rna,protein folding,gene expression,molecular,translation,ubiquitination,nucleic acids,ubiquitin ligase,apoptosis,nmr spectroscopy,rnai,zinc,dna replication,cell cycle,biophysics,macromolecules,protein binding,magnetic resonance spectroscopy,dna repair,mechanism,sequence alignment,negative feedback,dna recombination,protein turnover,signal transduction,chromatin,molecular biology,proteins,chromatin remodeling,transcription,chromatin structure,rna processing,protein conformation
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