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Chemical shift assignments of the N-terminal domain of PSD95 (PSD95-NT).
Zhang, Yonghong; Hell, Johannes W; Ames, James B.
Afiliação
  • Zhang Y; Department of Chemistry, University of California, Davis, CA, 95616, USA.
  • Hell JW; Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, 78539, USA.
  • Ames JB; Department of Pharmacology, University of California, Davis, CA, 95616, USA.
Biomol NMR Assign ; 15(2): 347-350, 2021 10.
Article em En | MEDLINE | ID: mdl-33929702
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).
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ressonância Magnética Nuclear Biomolecular Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ressonância Magnética Nuclear Biomolecular Idioma: En Ano de publicação: 2021 Tipo de documento: Article