1tp5: Difference between revisions
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== | ==Crystal structure of PDZ3 domain of PSD-95 protein complexed with a peptide ligand KKETWV== | ||
<StructureSection load='1tp5' size='340' side='right'caption='[[1tp5]], [[Resolution|resolution]] 1.54Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1tp5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TP5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.54Å</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=1tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tp5 OCA], [https://pdbe.org/1tp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1tp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tp5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DLG4_RAT DLG4_RAT] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B.<ref>PMID:15317815</ref> <ref>PMID:15358863</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/1tp5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tp5 ConSurf]. | |||
<div style="clear:both"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Kovari L]] | |||
[[Category: Kovari | [[Category: Martin P]] | ||
[[Category: Martin | [[Category: Paredes A]] | ||
[[Category: Paredes | [[Category: Saro D]] | ||
[[Category: Saro | [[Category: Spaller M]] | ||
[[Category: Spaller | [[Category: Vickrey J]] | ||
[[Category: Vickrey | [[Category: Wawrzak Z]] | ||
[[Category: Wawrzak | |||
Latest revision as of 09:32, 23 August 2023
Crystal structure of PDZ3 domain of PSD-95 protein complexed with a peptide ligand KKETWVCrystal structure of PDZ3 domain of PSD-95 protein complexed with a peptide ligand KKETWV
Structural highlights
FunctionDLG4_RAT Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B.[1] [2] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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