Chemical shift assignments of the N-terminal domain of PSD95 (PSD95-NT)

Yonghong Zhang, Johannes W. Hell, James B. Ames

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Postsynaptic density protein-95 (PSD95) contributes to the postsynaptic architecture of neuronal synapses and plays an important role in controlling synaptic plasticity. The N-terminal domain of PSD95 (residues 1–71, called PSD95-NT) interacts with target proteins (calmodulin, α-actinin-1 and CDKL5), which regulate the Ca2+-dependent degradation of glutamate receptors. We report complete backbone NMR chemical shift assignments of PSD95-NT (BMRB No. 50752).

Original languageEnglish (US)
Pages (from-to)347-350
Number of pages4
JournalBiomolecular NMR assignments
Volume15
Issue number2
DOIs
StatePublished - Oct 2021

Keywords

  • Calcium
  • Glutamate receptor
  • NMR
  • Postsynaptic density
  • PSD95

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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