PDBsum entry 3k82

Cell adhesion

PDB id: 3k82

Contents

Protein chain

98 a.a. *

Ligands

PO4

GOL

EPE

Waters ×84

* Residue conservation analysis

PDB id:

3k82

Name:

Cell adhesion

Title:

Crystal structure of the third pdz domain of psd-95

Structure:

Disks large homolog 4. Chain: a. Fragment: third pdz domain. Synonym: postsynaptic density protein 95, psd-95, synapse-associated protein 90, sap90. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.40Å R-factor: 0.174 R-free: 0.210

Authors:

A.Camara-Artigas,J.A.Gavira

Key ref:

A.Cámara-Artigas et al. (2010). Novel conformational aspects of the third PDZ domain of the neuronal post-synaptic density-95 protein revealed from two 1.4A X-ray structures. J Struct Biol, 170, 565-569. PubMed id: 20227506

Date:

13-Oct-09 Release date: 07-Apr-10

Protein chain

P78352  (DLG4_HUMAN) -  Disks large homolog 4 from Homo sapiens

Seq: 724 a.a.

Struc: 98 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

J Struct Biol 170:565-569 (2010)

PubMed id: 20227506

Novel conformational aspects of the third PDZ domain of the neuronal post-synaptic density-95 protein revealed from two 1.4A X-ray structures.

A.Cámara-Artigas, J.Murciano-Calles, J.A.Gavira, E.S.Cobos, J.C.Martínez.

ABSTRACT

The crystal structure of the third PDZ domain of the neuronal post-synaptic density-95 protein (PSD95-PDZ3, residues 302-402) has been solved at 1.4 and 1.35A from two different crystal forms. These structures lack the cloning artefact present in the carboxyl terminal sequence of the former crystallographic structures and they belong to the space groups P4(3) and P1. The new PDZ structures are identical between the two crystal forms and among the four chains of the P1 crystal form. When we compare the new structures with the previous ones, some important conformational differences in the C-terminal alpha-helix and in the loop connecting beta2 and beta3 strands have been found. Additionally, the high resolution of the new structures has allowed us to indentify a succinimide residue at the position corresponding to Asp332 in the beta2-beta3 loop, which may contribute to the alternate conformation of this loop, and at the same time, to the interaction between residues from this loop and the C-terminal alpha-helix. Thus, these features would have implications in the recently proposed allosteric role of this third alpha-helix in the binding of the carboxyl terminal fragments to the PSD95-PDZ3.