5hf4: Difference between revisions

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'''Unreleased structure'''


The entry 5hf4 is ON HOLD  until Paper Publication
==The third PDZ domain from the synaptic protein PSD-95 (H372A mutant)==
 
<StructureSection load='5hf4' size='340' side='right' caption='[[5hf4]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
Authors: White, K.I., Raman, A.S., Ranganathan, R.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5hf4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HF4 FirstGlance]. <br>
Description: The third PDZ domain from the synaptic protein PSD-95 (H372A mutant)
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bfe|1bfe]], [[5hdy|5hdy]], [[5heb|5heb]], [[5hed|5hed]], [[5het|5het]], [[5hey|5hey]], [[5hf1|5hf1]], [[5hfb|5hfb]], [[5hfc|5hfc]], [[5fhd|5fhd]], [[5hfe|5hfe]], [[5hff|5hff]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hf4 OCA], [http://pdbe.org/5hf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hf4 RCSB], [http://www.ebi.ac.uk/pdbsum/5hf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hf4 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Raman, A S]]
[[Category: Ranganathan, R]]
[[Category: Ranganathan, R]]
[[Category: Raman, A.S]]
[[Category: White, K I]]
[[Category: White, K.I]]
[[Category: Adhesion]]
[[Category: Dhr]]
[[Category: Glgf]]
[[Category: Pdz]]
[[Category: Peptide binding protein]]
[[Category: Peptide-binding domain]]
[[Category: Synapse]]
[[Category: Synaptic density]]

Revision as of 19:27, 18 January 2017

The third PDZ domain from the synaptic protein PSD-95 (H372A mutant)The third PDZ domain from the synaptic protein PSD-95 (H372A mutant)

Structural highlights

5hf4 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1] [2]

References

  1. Hruska-Hageman AM, Benson CJ, Leonard AS, Price MP, Welsh MJ. PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current. J Biol Chem. 2004 Nov 5;279(45):46962-8. Epub 2004 Aug 17. PMID:15317815 doi:10.1074/jbc.M405874200
  2. Prange O, Wong TP, Gerrow K, Wang YT, El-Husseini A. A balance between excitatory and inhibitory synapses is controlled by PSD-95 and neuroligin. Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13915-20. Epub 2004 Sep 9. PMID:15358863 doi:10.1073/pnas.0405939101

5hf4, resolution 1.75Å

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OCA