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- W2065989745 abstract "Modular PDZ domains, found in many cell junction–associated proteins, mediate the clustering of membrane ion channels by binding to their C-terminus. The X-ray crystallographic structures of the third PDZ domain from the synaptic protein PSD-95 in complex with and in the absence of its peptide ligand have been determined at 1.8 Å and 2.3 Å resolution, respectively. The structures reveal that a four-residue C-terminal stretch (X-Thr/Ser-X-Val-COO−) engages the PDZ domain through antiparallel main chain interactions with a β sheet of the domain. Recognition of the terminal carboxylate group of the peptide is conferred by a cradle of main chain amides provided by a Gly-Leu-Gly-Phe loop as well as by an arginine side chain. Specific side chain interactions and a prominent hydrophobic pocket explain the selective recognition of the C-terminal consensus sequence." @default.
- W2065989745 created "2016-06-24" @default.
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- W2065989745 date "1996-06-01" @default.
- W2065989745 modified "2023-10-12" @default.
- W2065989745 title "Crystal Structures of a Complexed and Peptide-Free Membrane Protein–Binding Domain: Molecular Basis of Peptide Recognition by PDZ" @default.
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- W2065989745 doi "https://doi.org/10.1016/s0092-8674(00)81307-0" @default.
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