PDBsum entry 1kef

Protein binding

PDB id: 1kef

Contents

Protein chain

93 a.a. *

* Residue conservation analysis

PDB id:

1kef

Name:

Protein binding

Title:

Pdz1 of sap90

Structure:

Synapse associated protein-90. Chain: a. Fragment: pdz1 domain. Synonym: (sap90), presynaptic density protein 95, psd-95. Engineered: yes

Source:

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

NMR struc:

1 models

Authors:

A.Piserchio,M.Pellegrini,S.Mehta,S.M.Blackman,E.P.Garcia,J.Marshall, D.F.Mierke

Key ref:

A.Piserchio et al. (2002). The PDZ1 domain of SAP90. Characterization of structure and binding. J Biol Chem, 277, 6967-6973. PubMed id: 11744724 DOI: 10.1074/jbc.M109453200

Date:

15-Nov-01 Release date: 06-Mar-02

Protein chain

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

Seq: 724 a.a.

Struc: 93 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1074/jbc.M109453200

J Biol Chem 277:6967-6973 (2002)

PubMed id: 11744724

The PDZ1 domain of SAP90. Characterization of structure and binding.

A.Piserchio, M.Pellegrini, S.Mehta, S.M.Blackman, E.P.Garcia, J.Marshall, D.F.Mierke.

ABSTRACT

The structural features of the PDZ1 domain of the synapse-associated protein SAP90 have been characterized by NMR. A comparison with the structures of the PDZ2 and PDZ3 domains of SAP90 illustrates significant differences, which may account for the unique binding properties of these homologous domains. Within the postsynaptic density, SAP90 functions as a molecular scaffold with a number of the protein-protein interactions mediated through the PDZ1 domain. Here, using fluorescence anisotropy and NMR chemical shift analysis, we have characterized the association of PDZ1 to the C-terminal peptides of the GluR6 subunit of the kainate receptor, voltage-gated K(+) channel Kv1.4, and microtubule-associate protein CRIPT, all of which are known to associate with SAP90. The latter two, which possess the consensus sequence for binding to PDZ domains (T/S-X-V-oh), have low micromolar binding affinities (1.5-15 microm). The C terminus of GluR6, RLPGKETMA-oh, lacking the consensus sequence, binds to PDZ1 of SAP90 with an affinity of 160 microm. The NMR data illustrate that although all three peptides occupy the binding groove capped by the GLGF loop of PDZ1, specific differences are present, consistent with the variation in binding affinities.

Selected figure(s)

Figure 1.
Fig. 1. 1H-15N HSQC spectrum of the PDZ1 domain of SAP90. Collected at 35 °C, pH 6.8 at 600 MHz.

Figure 3.
Fig. 3. One representative structure of the PDZ1 domain of SAP90 with the secondary structure elements highlighted.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2002, 277, 6967-6973) copyright 2002.

Figures were selected by an automated process.