Protein DJ-1

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== Structural highlights ==
== Structural highlights ==
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The 3D structure of DJ-1 complex with the inhibitor isatin shows the covalent bond formed between isatin and DJ-1 <scene name='86/864103/Cv/4'>conserved residue C106</scene> as well as the <scene name='86/864103/Cv/5'>numerous H-bonding interactions</scene> between the inhibitor and the protein<ref>PMID:30063823</ref>.
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The 3D structure of DJ-1 complex with the inhibitor isatin shows the covalent bond formed between isatin and DJ-1 <scene name='86/864103/Cv/4'>conserved residue C106</scene> as well as the <scene name='86/864103/Cv/5'>numerous H-bonding interactions</scene> between the inhibitor and the protein<ref>PMID:30063823</ref>. <scene name='86/864103/Cv/6'>Whole binding site</scene>. Water molecules are shown as red spheres.
==3D structures of protein DJ-1==
==3D structures of protein DJ-1==

Revision as of 12:04, 13 October 2020

Human DJ-1 complex with inhibitor isatin and Cl-1 (green) (PDB code 6afa).

Drag the structure with the mouse to rotate

References

  1. Junn E, Jang WH, Zhao X, Jeong BS, Mouradian MM. Mitochondrial localization of DJ-1 leads to enhanced neuroprotection. J Neurosci Res. 2009 Jan;87(1):123-9. doi: 10.1002/jnr.21831. PMID:18711745 doi:10.1002/jnr.21831
  2. Clements CM, McNally RS, Conti BJ, Mak TW, Ting JP. DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15091-6. Epub 2006 Oct 2. PMID:17015834 doi:10.1073/pnas.0607260103
  3. Chen J, Li L, Chin LS. Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage. Hum Mol Genet. 2010 Jun 15;19(12):2395-408. doi: 10.1093/hmg/ddq113. Epub 2010, Mar 18. PMID:20304780 doi:10.1093/hmg/ddq113
  4. Tashiro S, Caaveiro JMM, Nakakido M, Tanabe A, Nagatoishi S, Tamura Y, Matsuda N, Liu D, Hoang QQ, Tsumoto K. Discovery and Optimization of Inhibitors of the Parkinson's Disease Associated Protein DJ-1. ACS Chem Biol. 2018 Aug 15. doi: 10.1021/acschembio.8b00701. PMID:30063823 doi:http://dx.doi.org/10.1021/acschembio.8b00701

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Alexander Berchansky, Michal Harel

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