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TitleNicotinamide mononucleotide adenylyltransferase uses its NAD+substrate-binding site to chaperone phosphorylated Tau.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateFeb 5, 2018 (structure data deposition date)
AuthorsMa, X. / Zhu, Y. / Lu, J. / Xie, J. / Li, C. / Shin, W.S. / Qiang, J. / Liu, J. / Dou, S. / Xiao, Y. ...Ma, X. / Zhu, Y. / Lu, J. / Xie, J. / Li, C. / Shin, W.S. / Qiang, J. / Liu, J. / Dou, S. / Xiao, Y. / Wang, C. / Jia, C. / Long, H. / Yang, J. / Fang, Y. / Jiang, L. / Zhang, Y. / Zhang, S. / Zhai, R.G. / Liu, C. / Li, D.
External linksElife / PubMed:32250733
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-5z9r:
NMNAT as a specific chaperone antagonizing pathological condensation of phosphorylated tau
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsTRANSFERASE / antagonizing pathological condensation of phosphorylated tau / CHAPERONE

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