3tsv

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Current revision (13:38, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3tsv' size='340' side='right'caption='[[3tsv]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='3tsv' size='340' side='right'caption='[[3tsv]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tsv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TSV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tsv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TSV FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tsw|3tsw]], [[3tsz|3tsz]]</div></td></tr>
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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]] 1.989&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TJP1, ZO1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3tsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsv OCA], [https://pdbe.org/3tsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tsv RCSB], [https://www.ebi.ac.uk/pdbsum/3tsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsv 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=3tsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsv OCA], [https://pdbe.org/3tsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tsv RCSB], [https://www.ebi.ac.uk/pdbsum/3tsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ZO1_HUMAN ZO1_HUMAN]] The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells.<ref>PMID:21240187</ref>
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[https://www.uniprot.org/uniprot/ZO1_HUMAN ZO1_HUMAN] The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells.<ref>PMID:21240187</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tight junctions are cell-cell contacts that regulate the paracellular flux of solutes and prevent pathogen entry across cell layers. The assembly and permeability of this barrier is dependent on the Zonula Occludens (ZO) membrane-associated guanylate kinase (MAGUK) proteins ZO-1, -2, and -3. MAGUK proteins are characterized by a core motif of protein-binding domains that include a PDZ domain, a Src homology 3 (SH3) domain and a region of homology to guanylate kinase (GUK); the structure of this core motif has never been determined for any MAGUK. To better understand how ZO proteins organize the assembly of protein complexes we have crystallized the entire PDZ3-SH3-GUK core motif of ZO-1. We have also crystallized this core motif in complex with the cytoplasmic tail of the ZO-1 PDZ3 ligand, junctional adhesion molecule A (JAM-A) to determine how the activity of different domains is coordinated. Our study shows a new feature for PDZ class II ligand binding that implicates the two highly conserved Phe -2 and Ser -3 residues of JAM. Our X-ray structures and NMR experiments also show for the first time a role for adjacent domains in the binding of ligands to PDZ domains in the MAGUK proteins family.
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The Src Homology 3 Domain is Required for Junctional Adhesion Molecule Binding to the Third PDZ Domain of the Scaffolding Protein ZO-1.,Nomme J, Fanning AS, Caffrey M, Lye MF, Anderson JM, Lavie A J Biol Chem. 2011 Oct 26. PMID:22030391<ref>PMID:22030391</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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</div>
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<div class="pdbe-citations 3tsv" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lavie, A]]
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[[Category: Lavie A]]
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[[Category: Nomme, J]]
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[[Category: Nomme J]]
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[[Category: Cell adhesion]]
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[[Category: Jam]]
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[[Category: Pdz]]
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[[Category: Scaffolding]]
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[[Category: Tight junction]]
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Current revision

crystal structure of the third PDZ domain of the human ZO-1 MAGUK protein

PDB ID 3tsv

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