5mz7: Difference between revisions
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<StructureSection load='5mz7' size='340' side='right'caption='[[5mz7]], [[Resolution|resolution]] 1.53Å' scene=''> | <StructureSection load='5mz7' size='340' side='right'caption='[[5mz7]], [[Resolution|resolution]] 1.53Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5mz7]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5mz7]] is a 4 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=5MZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MZ7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZH:AZIDOHOMOALANINE'>AZH</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mz7 OCA], [https://pdbe.org/5mz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mz7 RCSB], [https://www.ebi.ac.uk/pdbsum/5mz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mz7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5mz7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5mz7" 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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kudlinzki | [[Category: Rattus norvegicus]] | ||
[[Category: Lehner | [[Category: Kudlinzki D]] | ||
[[Category: Linhard | [[Category: Lehner F]] | ||
[[Category: Schwalbe | [[Category: Linhard VL]] | ||
[[Category: Silvers | [[Category: Schwalbe H]] | ||
[[Category: Witt | [[Category: Silvers R]] | ||
[[Category: Witt K]] | |||
Latest revision as of 20:54, 8 November 2023
Crystal Structure of the third PDZ domain from the synaptic protein PSD-95 with incorporated AzidohomoalanineCrystal Structure of the third PDZ domain from the synaptic protein PSD-95 with incorporated Azidohomoalanine
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] Publication Abstract from PubMedThe impact of the incorporation of a non-natural amino acid (NNAA) onto protein structure, dynamics, and ligand binding has not been studied rigorously so far. NNAAs are regularly used to modify proteins post-translationally in vivo and in vitro using click-chemistry. Here, we present a structural characterization of the impact of the incorporation of azidohomoalanine (AZH) into the model protein domain PDZ3 using NMR spectroscopy and X-ray crystallography. The structure and dynamics of the apo state of the AZH-modified PDZ3 remains mostly unperturbed. Furthermore, the binding of two PDZ3 binding peptides are found to be unchanged by incorporation of AZH. We mapped the interface of the AZH-modified PDZ3 and an azulene-linked peptide for vibrational energy transfer studies using chemical shift perturbations and NOEs between the unlabelled azulene-linked peptide and the isotopically labelled protein. Co-crystallization and soaking failed for the peptide-bound holo-complex. NMR spectroscopy, however, al-lowed determination of the protein-ligand interface. While the incorpo-ration of AZH was minimally invasive for PDZ3, structural analysis of NNAA-modified proteins by the methodology presented here should be carried out to ensure structural integrity of the studied target. The Impact of Azidohomoalanine Incorporation on Protein Structure and Ligand Binding.,Lehner F, Kudlinzki D, Richter C, Muller-Werkmeister H, Eberl K, Bredenbeck J, Schwalbe H, Silvers R Chembiochem. 2017 Sep 26. doi: 10.1002/cbic.201700437. PMID:28950050[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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