2HE2

Crystal structure of the 3rd PDZ domain of human discs large homologue 2, DLG2

Summary for 2HE2

• Entry DOI: 10.2210/pdb2he2/pdb
• Descriptor: Discs large homolog 2 (2 entities in total)
• Functional Keywords: dlg2, pdz, pdz domain, signal transduction, structural genomics, structural genomics consortium, sgc, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Lipid-anchor (By similarity): Q15700
• Total number of polymer chains: 2
• Total formula weight: 21353.78

Authors

Turnbull, A.P.,Phillips, C.,Berridge, G.,Savitsky, P.,Smee, C.E.A.,Papagrigoriou, E.,Debreczeni, J.,Gorrec, F.,Elkins, J.M.,von Delft, F.,Weigelt, J.,Edwards, A.,Arrowsmith, C.,Sundstrom, M.,Doyle, D.A.,Structural Genomics Consortium (SGC) (deposition date: 2006-06-21, release date: 2006-07-04, Last modification date: 2023-08-30)

Primary citation

Elkins, J.M.,Papagrigoriou, E.,Berridge, G.,Yang, X.,Phillips, C.,Gileadi, C.,Savitsky, P.,Doyle, D.A.
Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions.
Protein Sci., 16:683-694, 2007

PubMed 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.

PubMed: 17384233
DOI: 10.1110/ps.062657507

Experimental method

X-RAY DIFFRACTION (1.5 Å)