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Molecular basis of Pirh2-mediated p53 ubiquitylation.

Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH,
Nature Structural & Molecular Biology (2008) 15:1334-42 PublishedPSI:Phase 2  
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. ...
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 
19043414  
10.1038/nsmb.1521  
56 (Last update: 11/10/2018 6:52:22pm)  
structure