2pdz: Difference between revisions

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-[[Image:2pdz.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2pdz", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_2pdz|  PDB=2pdz  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF THE SYNTROPHIN PDZ DOMAIN IN COMPLEX WITH THE PEPTIDE GVKESLV, NMR, 15 STRUCTURES'''
+==SOLUTION STRUCTURE OF THE SYNTROPHIN PDZ DOMAIN IN COMPLEX WITH THE PEPTIDE GVKESLV, NMR, 15 STRUCTURES==
+<StructureSection load='2pdz' size='340' side='right'caption='[[2pdz]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2pdz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PDZ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2pdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pdz OCA], [https://pdbe.org/2pdz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pdz RCSB], [https://www.ebi.ac.uk/pdbsum/2pdz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pdz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SNTA1_MOUSE SNTA1_MOUSE] Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate.
+== 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/pd/2pdz_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=2pdz ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Syntrophins are modular proteins belonging to the dystrophin associated glycoprotein complex and are thought to be involved in the regulation of the muscular system. Screening of peptide libraries revealed selectivity of the synotrophin PDZ domain toward the motif R/K/Q-E-S/T-X-V-COO- found to be highly conserved in the alpha-subunit C-terminus of vertebrate voltage gated sodium channels (VGSCs). The solution structure of the domain in complex with the peptide G-V-K-E-S-L-V shows specific interactions between the conserved residues in the peptide and syntrophin-characteristic residues in the domain. We propose that syntrophins localize VGSCs to the dystrophin network through its PDZ domain.
-==Overview==
+Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels.,Schultz J, Hoffmuller U, Krause G, Ashurst J, Macias MJ, Schmieder P, Schneider-Mergener J, Oschkinat H Nat Struct Biol. 1998 Jan;5(1):19-24. PMID:9437424<ref>PMID:9437424</ref>
-Syntrophins are modular proteins belonging to the dystrophin associated glycoprotein complex and are thought to be involved in the regulation of the muscular system. Screening of peptide libraries revealed selectivity of the synotrophin PDZ domain toward the motif R/K/Q-E-S/T-X-V-COO- found to be highly conserved in the alpha-subunit C-terminus of vertebrate voltage gated sodium channels (VGSCs). The solution structure of the domain in complex with the peptide G-V-K-E-S-L-V shows specific interactions between the conserved residues in the peptide and syntrophin-characteristic residues in the domain. We propose that syntrophins localize VGSCs to the dystrophin network through its PDZ domain.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-PDZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PDZ OCA].
+</div>
+<div class="pdbe-citations 2pdz" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels., Schultz J, Hoffmuller U, Krause G, Ashurst J, Macias MJ, Schmieder P, Schneider-Mergener J, Oschkinat H, Nat Struct Biol. 1998 Jan;5(1):19-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9437424 9437424]
+*[[Syntrophin|Syntrophin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Ashurst J]]
-[[Category: Ashurst, J.]]
+[[Category: Hoffmueller U]]
-[[Category: Hoffmueller, U.]]
+[[Category: Krause G]]
-[[Category: Krause, G.]]
+[[Category: Macias M]]
-[[Category: Macias, M.]]
+[[Category: Oschkinat H]]
-[[Category: Oschkinat, H.]]
+[[Category: Schmieder P]]
-[[Category: Schmieder, P.]]
+[[Category: Schneider-Mergener J]]
-[[Category: Schneider-Mergener, J.]]
+[[Category: Schultz J]]
-[[Category: Schultz, J.]]
-[[Category: Nmr]]
-[[Category: Syntrophin pdz domain]]
-[[Category: Voltage-gated sodium channel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:56:03 2008''