PDBsum entry 2dc2

Structural protein

PDB id: 2dc2

Contents

Protein chain

87 a.a. *

* Residue conservation analysis

PDB id:

2dc2

Name:

Structural protein

Title:

Solution structure of pdz domain

Structure:

Golgi associated pdz and coiled-coil motif containing isoform b. Chain: a. Fragment: pdz domain. Synonym: gopc. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: gopc gene (270-363). Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

X.Li,J.Wu,Y.Shi

Key ref:

X.Li et al. (2006). Solution structure of GOPC PDZ domain and its interaction with the C-terminal motif of neuroligin. Protein Sci, 15, 2149-2158. PubMed id: 16882988 DOI: 10.1110/ps.062087506

Date:

20-Dec-05 Release date: 26-Sep-06

Protein chain

Q9HD26  (GOPC_HUMAN) -  Golgi-associated PDZ and coiled-coil motif-containing protein from Homo sapiens

Seq: 462 a.a.

Struc: 87 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1110/ps.062087506

Protein Sci 15:2149-2158 (2006)

PubMed id: 16882988

Solution structure of GOPC PDZ domain and its interaction with the C-terminal motif of neuroligin.

X.Li, J.Zhang, Z.Cao, J.Wu, Y.Shi.

ABSTRACT

GOPC (Golgi-associated PDZ and coiled-coil motif-containing protein) represents a PDZ domain-containing protein associated with the Golgi apparatus, which plays important roles in vesicular trafficking in secretory and endocytic pathways. GOPC interacts with many other proteins, such as the Wnt receptors Frizzled 8 and neuroligin via its PDZ domain. Neuroligin is a neural cell-adhesion molecule of the post-synapse, which binds to the presynapse molecule neurexin to form a heterotypic intercellular junction. Here we report the solution structure of the GOPC PDZ domain by NMR. Our results show that it is a canonical class I PDZ domain, which contains two alpha-helices and six beta-strands. Using chemical shift perturbation experiments, we further studied the binding properties of the GOPC PDZ domain with the C-terminal motif of neuroligin. The observations showed that the ensemble of the interaction belongs to fast exchange with low affinity. The 3D model of the GOPC PDZ domain/neuroligin C-terminal peptide complex was constructed with the aid of the molecular dynamics simulation method. Our discoveries provide insight into the specific interaction of the GOPC PDZ domain with the C-terminal peptide of Nlg and also provide a general insight about the possible binding mode of the interaction of Nlg with other PDZ domain-containing proteins.

Selected figure(s)

Figure 4.
Figure 4. Histogram showing differences in chemical shifts in the free

Figure 6.
Figure 6. Nlg-binding site on the surface of the GOPC PDZ domain. (A) Surface conformation of the GOPC PDZ domain

The above figures are reprinted by permission from the Protein Society: Protein Sci (2006, 15, 2149-2158) copyright 2006.

Figures were selected by an automated process.