1iu0: Difference between revisions

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-[[Image:1iu0.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1iu0", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_1iu0|  PDB=1iu0  |  SCENE=  }}
-'''The first PDZ domain of PSD-95'''
+==The first PDZ domain of PSD-95==
+<StructureSection load='1iu0' size='340' side='right'caption='[[1iu0]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1iu0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IU0 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=1iu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iu0 OCA], [https://pdbe.org/1iu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1iu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iu0 ProSAT]</span></td></tr>
+</table>
+== 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>
+== 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/iu/1iu0_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=1iu0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+PDZ domain proteins play critical roles in binding, clustering and subcellular targeting of membrane receptors and ion channels. PDZ domains in multi-PDZ proteins often are arranged in groups with highly conserved spacing and intervening sequences; however, the functional significance of such tandem arrangements of PDZs is unclear. We have solved the three-dimensional structure of the first two PDZ domains of postsynaptic density protein-95 (PSD-95 PDZ1 and PDZ2), which are closely linked to each other in the PSD-95 family of scaffold proteins. The two PDZs have limited freedom of rotation and their C-terminal peptide-binding grooves are aligned with each other with an orientation preference for binding to pairs of C termini extending in the same direction. Increasing the spacing between PDZ1 and PDZ2 resulted in decreased binding between PDZ12 and its dimeric targets. The same mutation impaired the functional ability of PSD-95 to cluster Kv1.4 potassium channels in heterologous cells. The data presented provide a molecular basis for preferential binding of PSD-95 to multimeric membrane proteins with appropriate C-terminal sequences.
-==Overview==
+Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95.,Long JF, Tochio H, Wang P, Fan JS, Sala C, Niethammer M, Sheng M, Zhang M J Mol Biol. 2003 Mar 14;327(1):203-14. PMID:12614619<ref>PMID:12614619</ref>
-PDZ domain proteins play critical roles in binding, clustering and subcellular targeting of membrane receptors and ion channels. PDZ domains in multi-PDZ proteins often are arranged in groups with highly conserved spacing and intervening sequences; however, the functional significance of such tandem arrangements of PDZs is unclear. We have solved the three-dimensional structure of the first two PDZ domains of postsynaptic density protein-95 (PSD-95 PDZ1 and PDZ2), which are closely linked to each other in the PSD-95 family of scaffold proteins. The two PDZs have limited freedom of rotation and their C-terminal peptide-binding grooves are aligned with each other with an orientation preference for binding to pairs of C termini extending in the same direction. Increasing the spacing between PDZ1 and PDZ2 resulted in decreased binding between PDZ12 and its dimeric targets. The same mutation impaired the functional ability of PSD-95 to cluster Kv1.4 potassium channels in heterologous cells. The data presented provide a molecular basis for preferential binding of PSD-95 to multimeric membrane proteins with appropriate C-terminal sequences.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-IU0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IU0 OCA].
+</div>
+<div class="pdbe-citations 1iu0" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Supramodular structure and synergistic target binding of the N-terminal tandem PDZ domains of PSD-95., Long JF, Tochio H, Wang P, Fan JS, Sala C, Niethammer M, Sheng M, Zhang M, J Mol Biol. 2003 Mar 14;327(1):203-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12614619 12614619]
+*[[Postsynaptic density protein 3D structures|Postsynaptic density protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Long J-F]]
-[[Category: Long, J F.]]
+[[Category: Niethammer M]]
-[[Category: Niethammer, M.]]
+[[Category: Sala C]]
-[[Category: Sala, C.]]
+[[Category: Sheng M]]
-[[Category: Sheng, M.]]
+[[Category: Tochio H]]
-[[Category: Tochio, H.]]
+[[Category: Wang P]]
-[[Category: Wang, P.]]
+[[Category: Zhang M]]
-[[Category: Zhang, M.]]
-[[Category: Pdz domain]]
-[[Category: Post synaptic density]]
-[[Category: Psd-95]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:24:43 2008''