PDBsum entry 2he2

Signaling protein

PDB id: 2he2

Contents

Protein chains

102 a.a. *

Waters ×367

* Residue conservation analysis

PDB id:

2he2

Name:

Signaling protein

Title:

Crystal structure of the 3rd pdz domain of human discs large homologue 2, dlg2

Structure:

Discs large homolog 2. Chain: a, b. Synonym: postsynaptic density protein psd-93, channel- associated protein of synapse-110, chapsyn-110. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dlg2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.50Å R-factor: 0.130 R-free: 0.187

Authors:

A.P.Turnbull,C.Phillips,G.Berridge,P.Savitsky,C.E.A.Smee, E.Papagrigoriou,J.Debreczeni,F.Gorrec,J.M.Elkins,F.Von Delft, J.Weigelt,A.Edwards,C.Arrowsmith,M.Sundstrom,D.A.Doyle,Structural Genomics Consortium (Sgc)

Key ref:

J.M.Elkins et al. (2007). Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions. Protein Sci, 16, 683-694. PubMed id: 17384233 DOI: 10.1110/ps.062657507

Date:

21-Jun-06 Release date: 04-Jul-06

Protein chains

Q15700  (DLG2_HUMAN) -  Disks large homolog 2 from Homo sapiens

Seq: 870 a.a.

Struc: 102 a.a.*

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

DOI no: 10.1110/ps.062657507

Protein Sci 16:683-694 (2007)

PubMed id: 17384233

Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions.

J.M.Elkins, E.Papagrigoriou, G.Berridge, X.Yang, C.Phillips, C.Gileadi, P.Savitsky, D.A.Doyle.

ABSTRACT

PDZ domains are protein-protein interaction modules that generally bind to the C termini of their target proteins. The C-terminal four amino acids of a prospective binding partner of a PDZ domain are typically the determinants of binding specificity. In an effort to determine the structures of a number of PDZ domains we have included appropriate four residue extensions on the C termini of PDZ domain truncation mutants, designed for self-binding. Multiple truncations of each PDZ domain were generated. The four residue extensions, which represent known specificity sequences of the target PDZ domains and cover both class I and II motifs, form intermolecular contacts in the expected manner for the interactions of PDZ domains with protein C termini for both classes. We present the structures of eight unique PDZ domains crystallized using this approach and focus on four which provide information on selectivity (PICK1 and the third PDZ domain of DLG2), binding site flexibility (the third PDZ domain of MPDZ), and peptide-domain interactions (MPDZ 12th PDZ domain). Analysis of our results shows a clear improvement in the chances of obtaining PDZ domain crystals by using this approach compared to similar truncations of the PDZ domains without the C-terminal four residue extensions.

Selected figure(s)

Figure 2.
Figure 2. Ribbon diagrams of each of the 10 crystal forms (eight unique PDZ domains). The C-terminal four residues representing the PDZ recognition

Figure 6.
Figure 6. Crystal structure of MPDZ@3. (A) Superimposition of the structures of MPDZ@3 and MPDZ@7 showing the opposite

The above figures are reprinted by permission from the Protein Society: Protein Sci (2007, 16, 683-694) copyright 2007.

Figures were selected by an automated process.