PDBsum entry 4h11

Neuropeptide

PDB id: 4h11

Contents

Protein chains

102 a.a.

Ligands

SO4

ACT

Waters ×173

PDB id:

4h11

Name:

Neuropeptide

Title:

Interaction partners of psd-93 studied by x-ray crystallography and fluorescent polarization spectroscopy

Structure:

Disks large homolog 2. Chain: a, b. Fragment: pdz1: unp residues 93-188. Synonym: channel-associated protein of synapse-110, chapsyn-110, postsynaptic density protein psd-93. Engineered: yes

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: dlg2, dlgh2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.67Å R-factor: 0.174 R-free: 0.213

Authors:

M.Fiorentini,J.S.Kastrup,M.Gajhede

Key ref:

M.Fiorentini et al. (2013). Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy. Acta Crystallogr D Biol Crystallogr, 69, 587-594. PubMed id: 23519667 DOI: 10.1107/S0907444912051839

Date:

10-Sep-12 Release date: 03-Apr-13

Protein chains

Q63622  (DLG2_RAT) -  Disks large homolog 2 from Rattus norvegicus

Seq: 852 a.a.

Struc: 102 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S0907444912051839

Acta Crystallogr D Biol Crystallogr 69:587-594 (2013)

PubMed id: 23519667

Interaction partners of PSD-93 studied by X-ray crystallography and fluorescence polarization spectroscopy.

M.Fiorentini, A.Bach, K.Strømgaard, J.S.Kastrup, M.Gajhede.

ABSTRACT

PSD-93 (chapsyn-110, DLG2) is a member of the family of membrane-associated guanylate kinase (MAGUK) proteins. The MAGUK proteins are involved in receptor localization and signalling pathways. The best characterized MAGUK protein, PSD-95, is known to be involved in NMDA receptor signalling via its PDZ domains. The PDZ domains of PSD-95 and PSD-93 are structurally very similar, but relatively little is known about the function of PSD-93. PSD-93 has been suggested to interact with GluD2 from the family of ionotropic glutamate receptors. Here, the interactions of four residues (GTSI) representing the extreme C-terminus of GluD2 with PSD-93 PDZ1 have been investigated in the crystalline phase. Two different binding modes of these residues were observed, suggesting that the peptide is not tightly bound to PSD-93 PDZ1. In accordance, the two N-terminal PSD-93 PDZ domains show no appreciable binding affinity for a GluD2-derived C-terminal octapeptide, whereas micromolar affinity was observed for a GluN2B-derived C-terminal octapeptide. This indicates that if present, the interactions between GluD2 and PSD-93 involve more than the extreme terminus of the receptor. In contrast, the tumour-suppressor protein SCRIB PDZ3 shows low micromolar affinity towards the GluD2-derived octapeptide, which is in agreement with previous findings using high-throughput assays.