2BYG
2nd PDZ Domain of Discs Large Homologue 2
Summary for 2BYG
| Entry DOI | 10.2210/pdb2byg/pdb |
| Descriptor | CHANNEL ASSOCIATED PROTEIN OF SYNAPSE-110 (2 entities in total) |
| Functional Keywords | dlg2, pdz, pdz domain, structural genomics, structural genomics consortium, sgc, phosphorylation, sh3 domain, signal transduction |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cell membrane ; Lipid-anchor : Q15700 |
| Total number of polymer chains | 1 |
| Total formula weight | 12787.50 |
| Authors | Elkins, J.M.,Schoch, G.A.,Smee, C.E.A.,Berridge, G.,Salah, E.,Sundstrom, M.,Edwards, A.,Arrowsmith, C.,Weigelt, J.,Doyle, D.A.,Structural Genomics Consortium (SGC) (deposition date: 2005-08-01, release date: 2005-08-04, Last modification date: 2023-12-13) |
| Primary citation | Elkins, J.M.,Papagrigoriou, E.,Berridge, G.,Yang, X.,Phillips, C.,Gileadi, C.,Savitsky, C.,Doyle, D.A. Structure of Pick1 and Other Pdz Domains Obtained with the Help of Self-Binding C-Terminal Extensions. Protein Sci., 16:683-, 2007 Cited by 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: 17384233DOI: 10.1110/PS.062657507 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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