1BE9

THE THIRD PDZ DOMAIN FROM THE SYNAPTIC PROTEIN PSD-95 IN COMPLEX WITH A C-TERMINAL PEPTIDE DERIVED FROM CRIPT.

Summary for 1BE9

• Entry DOI: 10.2210/pdb1be9/pdb
• Descriptor: PSD-95, CRIPT (3 entities in total)
• Functional Keywords: peptide recognition, protein localization
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P31016
• Total number of polymer chains: 2
• Total formula weight: 13312.76

Authors

Doyle, D.A.,Lee, A.,Lewis, J.,Kim, E.,Sheng, M.,Mackinnon, R. (deposition date: 1998-05-20, release date: 1998-10-21, Last modification date: 2024-02-07)

Primary citation

Doyle, D.A.,Lee, A.,Lewis, J.,Kim, E.,Sheng, M.,MacKinnon, R.
Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ.
Cell(Cambridge,Mass.), 85:1067-1076, 1996

PubMed 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 angstroms and 2.3 angstroms 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 beta 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.

PubMed: 8674113
DOI: 10.1016/S0092-8674(00)81307-0

Experimental method

X-RAY DIFFRACTION (1.82 Å)