2K2C
Solution NMR structure of N-terminal domain of human pirh2. Northeast Structural Genomics Consortium (NESG) target HT2A
Summary for 2K2C
| Entry DOI | 10.2210/pdb2k2c/pdb |
| Related | 2K2D |
| NMR Information | BMRB: 15700 |
| Descriptor | RING finger and CHY zinc finger domain-containing protein 1, ZINC ION (2 entities in total) |
| Functional Keywords | zinc-binding protein, cytoplasm, metal-binding, nucleus, zinc-finger, metal binding protein, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 16297.69 |
| Authors | Wu, B.,Lemak, A.,Sheng, Y.,Karra, M.,Srisailam, S.,Sunnerhagen, M.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2008-03-31, release date: 2008-04-15, Last modification date: 2024-05-08) |
| Primary citation | Sheng, Y.,Laister, R.C.,Lemak, A.,Wu, B.,Tai, E.,Duan, S.,Lukin, J.,Sunnerhagen, M.,Srisailam, S.,Karra, M.,Benchimol, S.,Arrowsmith, C.H. Molecular basis of Pirh2-mediated p53 ubiquitylation. Nat.Struct.Mol.Biol., 15:1334-1342, 2008 Cited by PubMed Abstract: 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. PubMed: 19043414DOI: 10.1038/nsmb.1521 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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