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2xkx

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Revision as of 10:38, 12 January 2022

Single particle analysis of PSD-95 in negative stain

2xkx, resolution 22.90Å

Structural highlights

2xkx is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1tq3, 1rgr, 1iu2, 1jxm, 1kjw, 1tp3, 1be9, 1bfe, 1qlc, 1iu0, 1jxo, 1tp5, 2xky
Experimental data:	Check to display Experimental Data
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]

Publication Abstract from PubMed

The interaction of the extra-membranous domain of tetrameric inwardly rectifying Kir2.1 ion channels (Kir2.1NC(4)) with the membrane associated guanylate kinase protein PSD-95 has been studied using Transmission Electron Microscopy in negative stain. Three types of complexes were observed in electron micrographs corresponding to a 1:1 complex, a large self-enclosed tetrad complex and extended chains of linked channel domains. Using models derived from small angle X-ray scattering experiments in which high resolution structures from X-ray crystallographic and Nuclear Magnetic Resonance studies are positioned, the envelopes from single particle analysis can be resolved as a Kir2.1NC(4):PSD-95 complex and a tetrad of this unit (Kir2.1NC(4):PSD-95)(4). The tetrad complex shows the close association of the Kir2.1 cytoplasmic domains and the influence of PSD-95 mediated self-assembly on the clustering of these channels.

Self-directed assembly and clustering of the cytoplasmic domains of inwardly rectifying Kir2.1 potassium channels on association with PSD-95.,Fomina S, Howard TD, Sleator OK, Golovanova M, O'Ryan L, Leyland ML, Grossmann JG, Collins RF, Prince SM Biochim Biophys Acta. 2011 Jul 5;1808(10):2374-2389. PMID:21756874^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ Fomina S, Howard TD, Sleator OK, Golovanova M, O'Ryan L, Leyland ML, Grossmann JG, Collins RF, Prince SM. Self-directed assembly and clustering of the cytoplasmic domains of inwardly rectifying Kir2.1 potassium channels on association with PSD-95. Biochim Biophys Acta. 2011 Jul 5;1808(10):2374-2389. PMID:21756874 doi:10.1016/j.bbamem.2011.06.021

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xkx"

@@ Line 3: / Line 3: @@
 <SX load='2xkx' size='340' side='right' viewer='molstar' caption='[[2xkx]], [[Resolution|resolution]] 22.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xkx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XKX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XKX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xkx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XKX FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tq3|1tq3]], [[1rgr|1rgr]], [[1iu2|1iu2]], [[1jxm|1jxm]], [[1kjw|1kjw]], [[1tp3|1tp3]], [[1be9|1be9]], [[1bfe|1bfe]], [[1qlc|1qlc]], [[1iu0|1iu0]], [[1jxo|1jxo]], [[1tp5|1tp5]], [[2xky|2xky]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tq3|1tq3]], [[1rgr|1rgr]], [[1iu2|1iu2]], [[1jxm|1jxm]], [[1kjw|1kjw]], [[1tp3|1tp3]], [[1be9|1be9]], [[1bfe|1bfe]], [[1qlc|1qlc]], [[1iu0|1iu0]], [[1jxo|1jxo]], [[1tp5|1tp5]], [[2xky|2xky]]</div></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=2xkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xkx OCA], [http://pdbe.org/2xkx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xkx RCSB], [http://www.ebi.ac.uk/pdbsum/2xkx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xkx 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=2xkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xkx OCA], [https://pdbe.org/2xkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xkx RCSB], [https://www.ebi.ac.uk/pdbsum/2xkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xkx 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>
+[[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;">
 == Publication Abstract from PubMed ==

2xkx

From Proteopedia

Revision as of 10:38, 12 January 2022

Single particle analysis of PSD-95 in negative stain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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