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| | ==Solution Structure of Patj/Pals1 L27 Domain Complex== | | ==Solution Structure of Patj/Pals1 L27 Domain Complex== |
| - | <StructureSection load='1y76' size='340' side='right' caption='[[1y76]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1y76' size='340' side='right'caption='[[1y76]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y76]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Y76 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y74|1y74]]</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y76 OCA], [http://pdbe.org/1y76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y76 RCSB], [http://www.ebi.ac.uk/pdbsum/1y76 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y76 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=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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/MPP5_HUMAN MPP5_HUMAN]] May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity). | + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Feng, W]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Long, J F]] | + | [[Category: Feng W]] |
| - | [[Category: Zhang, M]] | + | [[Category: Long J-F]] |
| - | [[Category: Cell polarity]]
| + | [[Category: Zhang M]] |
| - | [[Category: L27 domain]]
| + | |
| - | [[Category: Protein assembly]]
| + | |
| - | [[Category: Scaffold protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
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.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Becamel C, Figge A, Poliak S, Dumuis A, Peles E, Bockaert J, Lubbert H, Ullmer C. Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 of the multi-PDZ domain protein MUPP1. J Biol Chem. 2001 Apr 20;276(16):12974-82. Epub 2001 Jan 9. PMID:11150294 doi:http://dx.doi.org/10.1074/jbc.M008089200
- ↑ Krapivinsky G, Medina I, Krapivinsky L, Gapon S, Clapham DE. SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase activity and NMDA receptor-dependent synaptic AMPA receptor potentiation. Neuron. 2004 Aug 19;43(4):563-74. PMID:15312654 doi:10.1016/j.neuron.2004.08.003
- ↑ Feng W, Long JF, Zhang M. A unified assembly mode revealed by the structures of tetrameric L27 domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold proteins. Proc Natl Acad Sci U S A. 2005 May 10;102(19):6861-6. Epub 2005 Apr 29. PMID:15863617
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