6SPV

Crystal structure of PDZ1-2 from PSD-95

Summary for 6SPV

• Entry DOI: 10.2210/pdb6spv/pdb
• Descriptor: Disks large homolog 4, GLUTATHIONE (3 entities in total)
• Functional Keywords: psd-95 fragment, clustering, protein-complex, receptor-binding, membrane associated, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 21175.99

Authors

Rodzli, N.,Levy, C.W.,Prince, S.M. (deposition date: 2019-09-02, release date: 2019-10-02, Last modification date: 2024-01-24)

Primary citation

Rodzli, N.A.,Lockhart-Cairns, M.P.,Levy, C.W.,Chipperfield, J.,Bird, L.,Baldock, C.,Prince, S.M.
The Dual PDZ Domain from Postsynaptic Density Protein 95 Forms a Scaffold with Peptide Ligand.
Biophys.J., 119:667-689, 2020

PubMed Abstract: PSD-95 is a member of the membrane-associated guanylate kinase class of proteins that forms scaffolding interactions with partner proteins, including ion and receptor channels. PSD-95 is directly implicated in modulating the electrical responses of excitable cells. The first two PSD-95/disks large/zona occludens (PDZ) domains of PSD-95 have been shown to be the key component in the formation of channel clusters. We report crystal structures of this dual domain in both apo- and ligand-bound form: thermodynamic analysis of the ligand association and small-angle x-ray scattering of the dual domain in the absence and presence of ligands. These experiments reveal that the ligated double domain forms a three-dimensional scaffold that can be described by a space group. The concentration of the components in this study is comparable with those found in compartments of excitable cells such as the postsynaptic density and juxtaparanodes of Ranvier. These in vitro experiments inform the basis of the scaffolding function of PSD-95 and provide a detailed model for scaffold formation by the PDZ domains of PSD-95.

PubMed: 32652058
DOI: 10.1016/j.bpj.2020.06.018

Experimental method

X-RAY DIFFRACTION (2.04 Å)