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Literature summary for extracted from

  • Ma, X.; Zhu, Y.; Lu, J.; Xie, J.; Li, C.; Shin, W.; 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.; Liu, C.; Li, D.
    Nicotinamide mononucleotide adenylyl transferase uses its NAD+ substrate-binding site to chaperone phosphorylated TAU (2020), eLife, 9, e51859 .
    View publication on PubMedView publication on EuropePMC


Cloned (Comment) Organism
expression in Escherichia coli Mus musculus
expression in Escherichia coli Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of isoform NMNAT3 to 2 A resolution Mus musculus

Protein Variants

Protein Variants Comment Organism
E198P/L217R mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
gel filtration Mus musculus


Organism UniProt Comment Textmining
Drosophila melanogaster Q9VC03 cf. EC
Mus musculus Q99JR6 isoform NMNAT3, cf. EC


Subunits Comment Organism
dimer 2 * 27700, calculated from sequence, and crystallization data Mus musculus


Synonyms Comment Organism
NMNAT3 cf. EC Mus musculus

General Information

General Information Comment Organism
physiological function NMNAT serves as a chaperone of phosphorylated Tau to prevent its amyloid aggregation in vitro as well as mitigate its pathology in Drosophila tauopathy models overexpressing human Tau. NMNAT adopts its enzymatic pocket to specifically bind the phosphorylated sites of Tau, which can be competitively disrupted by the enzymatic substrates of NMNAT. NMNAT serves as a cochaperone of Hsp90 for the specific recognition of phosphorylated Tau over Tau Drosophila melanogaster
physiological function NMNAT shows strong interaction with phosphorylated truncated Tau protein. The binding affinity of NMNAT3 to phosphorylated Tau is about one order of magnitude higher than that to Tau.The phosphorylated Ser residues of Tau are the primary binding sites. Substrates (i.e. NMN and ATP) and the chaperone client phosphorylated Tau share the same binding pocket with a partial overlap at the phosphate-binding site Mus musculus