Protein–protein interactions: PDZ domain networks
Open ArchiveDOI:https://doi.org/10.1016/S0960-9822(96)00737-3
Biochemical analyses using both in vivo and in vitro binding assays suggest that PDZ domains are modular protein-binding domains that have at least two distinct mechanisms for binding: they can bind to specific recognition sequences at the carboxyl termini of proteins, or they can dimerize with other PDZ domains. For example, the carboxyl termini of both the N-methyl D-aspartate (NMDA) receptor and the Shaker-type potassium channel have been identified as ligands for the first (PDZ 1) and second (PDZ 2) PDZ domains of three related proteins — the synapse-associated proteins PSD-95, chapsyn 110 and the human homolog of the Drosophila Dlg protein (hdlg) [
, , , ].
Biochemical analyses using both in vivo and in vitro binding assays suggest that PDZ domains are modular protein-binding domains that have at least two distinct mechanisms for binding: they can bind to specific recognition sequences at the carboxyl termini of proteins, or they can dimerize with other PDZ domains. For example, the carboxyl termini of both the N-methyl D-aspartate (NMDA) receptor and the Shaker-type potassium channel have been identified as ligands for the first (PDZ 1) and second (PDZ 2) PDZ domains of three related proteins — the synapse-associated proteins PSD-95, chapsyn 110 and the human homolog of the Drosophila Dlg protein (hdlg) [
, , , ].
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