2WL7
Crystal structure of the PSD93 PDZ1 domain
Summary for 2WL7
| Entry DOI | 10.2210/pdb2wl7/pdb |
| Descriptor | DISKS LARGE HOMOLOG 2, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | delta2 receptor interacting protein, transferase, dlg2, maguk, psd93, pdz domain, chapsyn-110 |
| Biological source | MUS MUSCULUS (MOUSE) |
| Cellular location | Membrane; Lipid-anchor (By similarity): Q91XM9 |
| Total number of polymer chains | 1 |
| Total formula weight | 11277.97 |
| Authors | Fiorentini, M.,Kallehauge, A.,Kristensen, O.,Kastrup, J.S.,Gajhede, M. (deposition date: 2009-06-22, release date: 2010-01-19, Last modification date: 2023-12-13) |
| Primary citation | Fiorentini, M.,Nielsen, A.K.,Kristensen, O.,Kastrup, J.S.,Gajhede, M. Structure of the First Pdz Domain of Human Psd-93. Acta Crystallogr.,Sect.F, 65:1254-, 2009 Cited by PubMed Abstract: The crystal structure of the PDZ1 domain of human PSD-93 has been determined to 2.0 A resolution. The PDZ1 domain forms a crystallographic trimer that is also predicted to be stable in solution. The main contributions to the stabilization of the trimer seem to arise from interactions involving the PDZ1-PDZ2 linker region at the extreme C-terminus of PDZ1, implying that the oligomerization that is observed is not of biological significance in full-length PSD-93. Comparison of the structures of the binding cleft of PSD-93 PDZ1 with the previously reported structures of PSD-93 PDZ2 and PDZ3 as well as of the closely related human PSD-95 PDZ1 shows that they are very similar in terms of amino-acid composition. However, the cleft is significantly narrower in PSD-95. This could be part of the basis of peptide selectivity between PSD-93 PDZ1 and PSD-95 PDZ1. PubMed: 20054121DOI: 10.1107/S1744309109043267 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.028 Å) |
Structure validation
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