1y76

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{{Seed}}
 
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[[Image:1y76.png|left|200px]]
 
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==Solution Structure of Patj/Pals1 L27 Domain Complex==
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The line below this paragraph, containing "STRUCTURE_1y76", creates the "Structure Box" on the page.
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<StructureSection load='1y76' size='340' side='right'caption='[[1y76]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1y76]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y76 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1y76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y76 OCA], [https://pdbe.org/1y76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y76 RCSB], [https://www.ebi.ac.uk/pdbsum/1y76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y76 ProSAT]</span></td></tr>
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{{STRUCTURE_1y76| PDB=1y76 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MPDZ_RAT MPDZ_RAT] Interacts with HTR2C and provokes its clustering at the cell surface. Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses.<ref>PMID:11150294</ref> <ref>PMID:15312654</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y7/1y76_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1y76 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Initially identified in Caenorhabditis elegans Lin-2 and Lin-7, L27 domain is a protein-protein interaction domain capable of organizing scaffold proteins into supramolecular assemblies by formation of heteromeric L27 domain complexes. L27 domain-mediated protein assemblies have been shown to play essential roles in cellular processes including asymmetric cell division, establishment and maintenance of cell polarity, and clustering of receptors and ion channels. The structural basis of L27 domain heteromeric complex assembly is controversial. We determined the high-resolution solution structure of the prototype L27 domain complex formed by mLin-2 and mLin-7 as well as the solution structure of the L27 domain complex formed by Patj and Pals1. The structures suggest that a tetrameric structure composed of two units of heterodimer is a general assembly mode for cognate pairs of L27 domains. Structural analysis of the L27 domain complex structures further showed that the central four-helix bundles mediating tetramer assembly are highly distinct between different pairs of L27 domain complexes. Biochemical studies revealed that the C-terminal alpha-helix responsible for the formation of the central helix bundle is a critical specificity determinant for each L27 domain in choosing its binding partner. Our results provide a unified picture for L27 domain-mediated protein-protein interactions.
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===Solution Structure of Patj/Pals1 L27 Domain Complex===
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A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins.,Feng W, Long JF, Zhang M Proc Natl Acad Sci U S A. 2005 May 10;102(19):6861-6. Epub 2005 Apr 29. PMID:15863617<ref>PMID:15863617</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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The line below this paragraph, {{ABSTRACT_PUBMED_15863617}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1y76" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15863617 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15863617}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1Y76 is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y76 OCA].
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==Reference==
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<ref group="xtra">PMID:15863617</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Feng, W.]]
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[[Category: Feng W]]
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[[Category: Long, J F.]]
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[[Category: Long J-F]]
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[[Category: Zhang, M.]]
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[[Category: Zhang M]]
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[[Category: Cell polarity]]
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[[Category: L27 domain]]
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[[Category: Protein assembly]]
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[[Category: Scaffold protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:58:31 2009''
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Current revision

Solution Structure of Patj/Pals1 L27 Domain Complex

PDB ID 1y76

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OCA

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