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

Yonghong Zhang; Johannes W Hell; James B Ames

doi:10.1007/s12104-021-10028-5

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

Biomol NMR Assign. 2021 Oct;15(2):347-350. doi: 10.1007/s12104-021-10028-5. Epub 2021 Apr 30.

Authors

Yonghong Zhang^{1

2}, Johannes W Hell³, James B Ames⁴

Affiliations

¹ Department of Chemistry, University of California, Davis, CA, 95616, USA.
² Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, 78539, USA.
³ Department of Pharmacology, University of California, Davis, CA, 95616, USA.
⁴ Department of Chemistry, University of California, Davis, CA, 95616, USA. jbames@ucdavis.edu.

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).

Keywords: Calcium; Glutamate receptor; NMR; PSD95; Postsynaptic density.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Disks Large Homolog 4 Protein* / chemistry
Disks Large Homolog 4 Protein* / metabolism
Nuclear Magnetic Resonance, Biomolecular*
Protein Domains*

Substances

Disks Large Homolog 4 Protein

Abstract

Publication types

MeSH terms

Substances

Grants and funding