1vf6

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[[Image:1vf6.jpg|left|200px]]
 
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==2.1 Angstrom crystal structure of the PALS-1-L27N and PATJ L27 heterodimer complex==
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The line below this paragraph, containing "STRUCTURE_1vf6", creates the "Structure Box" on the page.
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<StructureSection load='1vf6' size='340' side='right'caption='[[1vf6]], [[Resolution|resolution]] 2.10&Aring;' 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'>[[1vf6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VF6 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">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=1vf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vf6 OCA], [https://pdbe.org/1vf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vf6 ProSAT]</span></td></tr>
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{{STRUCTURE_1vf6| PDB=1vf6 | SCENE= }}
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</table>
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== Function ==
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'''2.1 Angstrom crystal structure of the PALS-1-L27N and PATJ L27 heterodimer complex'''
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[https://www.uniprot.org/uniprot/INADL_HUMAN INADL_HUMAN] Scaffolding protein that may bring different proteins into adjacent positions at the cell membrane. May regulate protein targeting, cell polarity and integrity of tight junctions. May regulate the surface expression and/or function of ASIC3 in sensory neurons.<ref>PMID:11927608</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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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/vf/1vf6_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=1vf6 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 ==
L27 is a protein-binding domain that can assemble essential proteins for signaling and cell polarity into complexes by interacting in a heterodimeric manner. One of these protein complexes is the PATJ/PALS1/Crumbs tripartite complex, which is crucial for the establishment and maintenance of cell polarity. To reveal the structural basis underlining the obligate heterodimerization, we have determined the crystal structure of the PALS1-L27N/PATJ-L27 heterodimer complex. Each L27 domain is composed of three helices. The two L27 domains heterodimerize by building a compact structure consisting of a four-helix bundle formed by the first two helices of each L27 domain and one coiled-coil formed by the third helix of each domain. The large hydrophobic packing interactions contributed by all the helices of both L27 domains predominantly drive the heterodimer formation, which is likely to be a general feature of L27 domains. Combined with mutational studies, we can begin to understand the structural basis for the specificity of L27 binding pairs. Our results provide unique insights into L27 domain heterodimer complex, which is critical for cell polarization.
L27 is a protein-binding domain that can assemble essential proteins for signaling and cell polarity into complexes by interacting in a heterodimeric manner. One of these protein complexes is the PATJ/PALS1/Crumbs tripartite complex, which is crucial for the establishment and maintenance of cell polarity. To reveal the structural basis underlining the obligate heterodimerization, we have determined the crystal structure of the PALS1-L27N/PATJ-L27 heterodimer complex. Each L27 domain is composed of three helices. The two L27 domains heterodimerize by building a compact structure consisting of a four-helix bundle formed by the first two helices of each L27 domain and one coiled-coil formed by the third helix of each domain. The large hydrophobic packing interactions contributed by all the helices of both L27 domains predominantly drive the heterodimer formation, which is likely to be a general feature of L27 domains. Combined with mutational studies, we can begin to understand the structural basis for the specificity of L27 binding pairs. Our results provide unique insights into L27 domain heterodimer complex, which is critical for cell polarization.
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==About this Structure==
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Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes.,Li Y, Karnak D, Demeler B, Margolis B, Lavie A EMBO J. 2004 Jul 21;23(14):2723-33. Epub 2004 Jul 8. PMID:15241471<ref>PMID:15241471</ref>
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1VF6 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VF6 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural basis for L27 domain-mediated assembly of signaling and cell polarity complexes., Li Y, Karnak D, Demeler B, Margolis B, Lavie A, EMBO J. 2004 Jul 21;23(14):2723-33. Epub 2004 Jul 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15241471 15241471]
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</div>
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<div class="pdbe-citations 1vf6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Protein complex]]
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[[Category: Karnak D]]
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[[Category: Karnak, D.]]
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[[Category: Lavie A]]
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[[Category: Lavie, A.]]
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[[Category: Li Y]]
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[[Category: Li, Y.]]
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[[Category: Margolis B]]
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[[Category: Margolis, B.]]
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[[Category: Coiled-coil]]
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[[Category: Four-helical bundle]]
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[[Category: Heterodimer]]
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[[Category: Hydrophobic packing interaction]]
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[[Category: L27 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:28:16 2008''
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Current revision

2.1 Angstrom crystal structure of the PALS-1-L27N and PATJ L27 heterodimer complex

PDB ID 1vf6

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