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| | <StructureSection load='2wl7' size='340' side='right'caption='[[2wl7]], [[Resolution|resolution]] 2.03Å' scene=''> | | <StructureSection load='2wl7' size='340' side='right'caption='[[2wl7]], [[Resolution|resolution]] 2.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wl7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WL7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WL7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.028Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Guanylate_kinase Guanylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.8 2.7.4.8] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wl7 OCA], [http://pdbe.org/2wl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wl7 RCSB], [http://www.ebi.ac.uk/pdbsum/2wl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wl7 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wl7 OCA], [https://pdbe.org/2wl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wl7 RCSB], [https://www.ebi.ac.uk/pdbsum/2wl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wl7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DLG2_MOUSE DLG2_MOUSE] Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses.<ref>PMID:12890763</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 2wl7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2wl7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Postsynaptic density protein 3D structures|Postsynaptic density protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Guanylate kinase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Fiorentini, M]] | + | [[Category: Fiorentini M]] |
| - | [[Category: Gajhede, M]] | + | [[Category: Gajhede M]] |
| - | [[Category: Kallehauge, A]] | + | [[Category: Kallehauge A]] |
| - | [[Category: Kastrup, J S]] | + | [[Category: Kastrup JS]] |
| - | [[Category: Kristensen, O]] | + | [[Category: Kristensen O]] |
| - | [[Category: Chapsyn-110]]
| + | |
| - | [[Category: Delta2 receptor interacting protein]]
| + | |
| - | [[Category: Dlg2]]
| + | |
| - | [[Category: Maguk]]
| + | |
| - | [[Category: Pdz domain]]
| + | |
| - | [[Category: Psd93]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
DLG2_MOUSE Required for perception of chronic pain through NMDA receptor signaling. Regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord. Interacts with the cytoplasmic tail of NMDA receptor subunits as well as inward rectifying potassium channels. Involved in regulation of synaptic stability at cholinergic synapses. Part of the postsynaptic protein scaffold of excitatory synapses.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of the first PDZ domain of human PSD-93.,Fiorentini M, Nielsen AK, Kristensen O, Kastrup JS, Gajhede M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1254-7. Epub 2009 Nov 27. PMID:20054121[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tao YX, Rumbaugh G, Wang GD, Petralia RS, Zhao C, Kauer FW, Tao F, Zhuo M, Wenthold RJ, Raja SN, Huganir RL, Bredt DS, Johns RA. Impaired NMDA receptor-mediated postsynaptic function and blunted NMDA receptor-dependent persistent pain in mice lacking postsynaptic density-93 protein. J Neurosci. 2003 Jul 30;23(17):6703-12. PMID:12890763 doi:10.1523/JNEUROSCI.23-17-06703.2003
- ↑ Fiorentini M, Nielsen AK, Kristensen O, Kastrup JS, Gajhede M. Structure of the first PDZ domain of human PSD-93. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt, 12):1254-7. Epub 2009 Nov 27. PMID:20054121 doi:10.1107/S1744309109043267
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