(Q30010229)

English

Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK).

scientific article published on 30 September 2011

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scholarly article

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13 February 2020

Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK) (English)

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13 February 2020

phosphorylation

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1

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13 February 2020

author name string

Chad M Petit

2

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13 February 2020

David S King

3

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13 February 2020

Andrew L Lee

4

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30 September 2011

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13 February 2020

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10

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Journal of Biological Chemistry

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13 February 2020

41776-41785

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48

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13 February 2020

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Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95

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Structural characterization of the intramolecular interaction between the SH3 and guanylate kinase domains of PSD-95

1 reference

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1 reference

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Phosphorylation of the AMPA receptor subunit GluR2 differentially regulates its interaction with PDZ domain-containing proteins

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Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ

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1 reference

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inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M111.272583

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Europe PubMed Central

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13 February 2020

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13 February 2020

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Europe PubMed Central

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13 February 2020

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