|Nature Structural & Molecular Biology (2008) 15:1334-42|
|Northeast Structural Genomics Consortium|
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Pirh2 (p53-induced RING-H2 domain protein; also known as Rchy1) is an E3 ubiquitin ligase involved in a negative-feedback loop with p53. ...
Using NMR spectroscopy, we show that Pirh2 is a unique cysteine-rich protein comprising three modular domains. The protein binds nine zinc ions using a variety of zinc coordination schemes, including a RING domain and a left-handed beta-spiral in which three zinc ions align three consecutive small beta-sheets in an interleaved fashion. We show that Pirh2-p53 interaction is dependent on the C-terminal zinc binding module of Pirh2, which binds to the tetramerization domain of p53. As a result, Pirh2 preferentially ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting that Pirh2 regulates protein turnover of the transcriptionally active form of p53.
|metabolism chemistry |
|Protein Structure, Tertiary Amino Acid Sequence Models, Molecular Molecular Sequence Data Protein Binding Sequence Alignment Protein Conformation Ubiquitin-Protein Ligases Magnetic Resonance Spectroscopy Protein Interaction Mapping Tumor Suppressor Protein p53 Protein Interaction Domains and Motifs Ubiquitination |
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