3qe1

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<StructureSection load='3qe1' size='340' side='right'caption='[[3qe1]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
<StructureSection load='3qe1' size='340' side='right'caption='[[3qe1]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qe1]] is a 1 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=3QE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QE1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qe1]] is a 1 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=3QE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QE1 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qdo|3qdo]], [[3qgl|3qgl]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mrt1, Kcnj9 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe1 OCA], [https://pdbe.org/3qe1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qe1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qe1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qe1 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=3qe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe1 OCA], [https://pdbe.org/3qe1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qe1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qe1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qe1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SNX27_RAT SNX27_RAT]] Involved in endocytic trafficking (By similarity). In T lymphocytes, participates in endocytic recycling pathway. Recruits PSCDBP and HT4R to early endosomes (By similarity).
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[https://www.uniprot.org/uniprot/KCNJ9_RAT KCNJ9_RAT] This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity).[https://www.uniprot.org/uniprot/SNX27_RAT SNX27_RAT] Involved in endocytic trafficking (By similarity). In T lymphocytes, participates in endocytic recycling pathway. Recruits PSCDBP and HT4R to early endosomes (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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G protein-gated inwardly rectifying potassium (GIRK) channels are important gatekeepers of neuronal excitability. The surface expression of neuronal GIRK channels is regulated by the psychostimulant-sensitive sorting nexin 27 (SNX27) protein through a class I (-X-Ser/Thr-X-Phi, where X is any residue and Phi is a hydrophobic amino acid) PDZ-binding interaction. The G protein-insensitive inward rectifier channel (IRK1) contains the same class I PDZ-binding motif but associates with a different synaptic PDZ protein, postsynaptic density protein 95 (PSD95). The mechanism by which SNX27 and PSD95 discriminate these channels was previously unclear. Using high-resolution structures coupled with biochemical and functional analyses, we identified key amino acids upstream of the channel's canonical PDZ-binding motif that associate electrostatically with a unique structural pocket in the SNX27-PDZ domain. Changing specific charged residues in the channel's carboxyl terminus or in the PDZ domain converts the selective association and functional regulation by SNX27. Elucidation of this unique interaction site between ion channels and PDZ-containing proteins could provide a therapeutic target for treating brain diseases.
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Mechanism underlying selective regulation of G protein-gated inwardly rectifying potassium channels by the psychostimulant-sensitive sorting nexin 27.,Balana B, Maslennikov I, Kwiatkowski W, Stern KM, Bahima L, Choe S, Slesinger PA Proc Natl Acad Sci U S A. 2011 Mar 21. PMID:21422294<ref>PMID:21422294</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qe1" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Balana, B]]
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[[Category: Rattus norvegicus]]
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[[Category: Choe, S]]
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[[Category: Balana B]]
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[[Category: Kwiatkowski, W]]
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[[Category: Choe S]]
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[[Category: Brain]]
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[[Category: Kwiatkowski W]]
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[[Category: Early endosome]]
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[[Category: Girk3 regulation]]
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[[Category: Neuron]]
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[[Category: Pdz binding]]
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[[Category: Pdz domain]]
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[[Category: Protein binding]]
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Current revision

Crystal Structure of PDZ domain of sorting nexin 27 (SNX27) fused to the C-terminal residues (ESESKV) of GIRK3

PDB ID 3qe1

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