1N7E

Crystal structure of the sixth PDZ domain of GRIP1

Summary for 1N7E

• Entry DOI: 10.2210/pdb1n7e/pdb
• Related: 1N7F
• Descriptor: AMPA receptor interacting protein GRIP (2 entities in total)
• Functional Keywords: pdz, grip, protein binding
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P97879
• Total number of polymer chains: 1
• Total formula weight: 10142.64

Authors

Im, Y.J.,Park, S.H.,Rho, S.H.,Lee, J.H.,Kang, G.B.,Sheng, M.,Kim, E.,Eom, S.H. (deposition date: 2002-11-14, release date: 2003-08-12, Last modification date: 2024-03-13)

Primary citation

Im, Y.J.,Park, S.H.,Rho, S.H.,Lee, J.H.,Kang, G.B.,Sheng, M.,Kim, E.,Eom, S.H.
Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization
J.BIOL.CHEM., 278:8501-8507, 2003

PubMed Abstract: PDZ domains bind to short segments within target proteins in a sequence-specific fashion. Glutamate receptor-interacting protein (GRIP)/ABP family proteins contain six to seven PDZ domains and interact via the sixth PDZ domain (class II) with the C termini of various proteins including liprin-alpha. In addition the PDZ456 domain mediates the formation of homo- and heteromultimers of GRIP proteins. To better understand the structural basis of peptide recognition by a class II PDZ domain and PDZ-mediated multimerization, we determined the crystal structures of the GRIP1 PDZ6 domain alone and in complex with a synthetic C-terminal octapeptide of human liprin-alpha at resolutions of 1.5 and 1.8 A, respectively. Remarkably, unlike other class II PDZ domains, Ile-736 at alphaB5 rather than conserved Leu-732 at alphaB1 makes a direct hydrophobic contact with the side chain of the Tyr at the -2 position of the ligand. Moreover, the peptide-bound structure of PDZ6 shows a slight reorientation of helix alphaB, indicating that the second hydrophobic pocket undergoes a conformational adaptation to accommodate the bulkiness of the Tyr side chain, and forms an antiparallel dimer through an interface located at a site distal to the peptide-binding groove. This configuration may enable formation of GRIP multimers and efficient clustering of GRIP-binding proteins.

PubMed: 12493751
DOI: 10.1074/jbc.M212263200

Experimental method

X-RAY DIFFRACTION (1.5 Å)