1P1E

Structural Insights into the Inter-domain Chaperoning of Tandem PDZ Domains in Glutamate Receptor Interacting Proteins

Summary for 1P1E

• Entry DOI: 10.2210/pdb1p1e/pdb
• Related: 1P1D
• Descriptor: Glutamate receptor interacting protein (1 entity in total)
• Functional Keywords: pdz domain, glutamate receptor, chaperoning domain, protein binding
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P97879
• Total number of polymer chains: 1
• Total formula weight: 10832.94

Authors

Feng, W.,Shi, Y.,Li, M.,Zhang, M. (deposition date: 2003-04-12, release date: 2003-11-11, Last modification date: 2024-05-29)

Primary citation

Feng, W.,Shi, Y.,Li, M.,Zhang, M.
Tandem PDZ repeats in glutamate receptor-interacting proteins have a novel mode of PDZ domain-mediated target binding
Nat.Struct.Biol., 10:972-978, 2003

PubMed Abstract: The interaction of the glutamate receptor subunits 2 and 3 (GluR2/3) with multi-PDZ domain glutamate receptor-interacting protein (GRIP) is important for the synaptic trafficking and clustering of the receptors. Binding of GluR2/3 to GRIP requires both the fourth and fifth PDZ domains (PDZ4 and PDZ5) to be covalently linked, although only one PDZ domain is directly involved in binding to the receptor tail. To elucidate the molecular basis of this mode of PDZ domain-mediated target recognition, we solved the solution structures of the PDZ45 tandem and the isolated PDZ4 of GRIP. The two PDZ domains form a compact structure with a fixed interdomain orientation. The interdomain packing and the stable folding of both PDZ domains require a short stretch of amino acids N-terminal to PDZ4 and a conserved linker connecting PDZ4 and PDZ5. PDZ4 contains a deformed aB-bB groove that is unlikely to bind to carboxyl peptides. Instead, the domain stabilizes the structure of PDZ5.

PubMed: 14555997
DOI: 10.1038/nsb992

Experimental method

SOLUTION NMR