PDBsum entry 2ev8

Membrane protein

PDB id: 2ev8

Contents

Protein chain

85 a.a. *

* Residue conservation analysis

PDB id:

2ev8

Name:

Membrane protein

Title:

Solution structure of the erythroid p55 pdz domain

Structure:

55 kda erythrocyte membrane protein. Chain: a. Fragment: pdz domain, residues 69-153. Synonym: erythroid p55, p55, membrane protein, palmitoylated 1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

H.Kusunoki,T.Kohno

Key ref:

H.Kusunoki and T.Kohno (2006). Solution structure of human erythroid p55 PDZ domain. Proteins, 64, 804-807. PubMed id: 16741958 DOI: 10.1002/prot.21028

Date:

31-Oct-05 Release date: 10-Oct-06

Protein chain

Q00013  (EM55_HUMAN) -  55 kDa erythrocyte membrane protein from Homo sapiens

Seq: 466 a.a.

Struc: 85 a.a.

DOI no: 10.1002/prot.21028

Proteins 64:804-807 (2006)

PubMed id: 16741958

Solution structure of human erythroid p55 PDZ domain.

H.Kusunoki, T.Kohno.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Solution structure of the p55 PDZ domain. (A) Stereo view of the 20 final structures of the p55 PDZ domain (residues 69-153). The superposition of the backbone atoms (N, C , and C ) is shown. (B) Ribbon diagram of the energy-minimized average structure of the p55 PDZ domain. The -helices are shown in red, and the -strands are cyan. The secondary structure elements are labeled according to the scheme used in the crystal structure of PSD95 PDZ3.[8] (C) Superposition of the PDZ domain of p55 (blue) with those of PSD95-PDZ3^8 (red), hCASK^10 (green), InaD[27] (yellow), GRIP1-PDZ6[28] (cyan), and AF-6[29] (purple). (D) Space-filling model of the groove between strand B and helix B of the p55 PDZ domain. Basic, acidic and hydrophobic amino acids are shown in blue, red and yellow, respectively. (E) Identification of the GPC-binding site on the p55 PDZ domain by the chemical shift perturbation experiment. The residues (Gly83, Thr85, Leu86, Leu88, Val125, Ser129, Val130, Gln134, Met137, and Glu139) showing large chemical shift changes caused by the addition of a 10-fold molar excess of peptide are labeled and colored purple. With the exception of Val125, all of these residues reside on one side of the protein surface.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 64, 804-807) copyright 2006.