5n7i
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Crystal structure of the coiled-coil domain of human tricellulin== |
| + | <StructureSection load='5n7i' size='340' side='right' caption='[[5n7i]], [[Resolution|resolution]] 2.88Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5n7i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N7I FirstGlance]. <br> | ||
| + | </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=5n7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n7i OCA], [http://pdbe.org/5n7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n7i RCSB], [http://www.ebi.ac.uk/pdbsum/5n7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n7i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/MALD2_HUMAN MALD2_HUMAN]] Autosomal recessive non-syndromic sensorineural deafness type DFNB. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MALD2_HUMAN MALD2_HUMAN]] Plays a role in the formation of the epithelial barriers. The separation of the endolymphatic and perilymphatic spaces of the organ of Corti from one another by epithelial barriers is required for normal hearing.<ref>PMID:17186462</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tricellulin is a tight junction protein localized to tricellular contacts in many epithelial tissues, where it is required for full barrier control. Here, we present crystal structures of the tricellulin C-terminal coiled-coil domain, revealing a potential dimeric arrangement. By combining structural, biochemical, functional, and mutation analyses, we gain insight into the mode of tricellulin oligomerization and suggest a model where dimerization of its cytoplasmic C-terminus may play an auxiliary role in stabilizing homophilic and potentially also heterophilic cis-interactions within tight junctions. | ||
| - | + | Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.,Schuetz A, Radusheva V, Krug SM, Heinemann U Ann N Y Acad Sci. 2017 Jun 29. doi: 10.1111/nyas.13408. PMID:28661558<ref>PMID:28661558</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 5n7i" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Heinemann, U]] | [[Category: Heinemann, U]] | ||
[[Category: Schuetz, A]] | [[Category: Schuetz, A]] | ||
| + | [[Category: Cc domain]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Dimerization]] | ||
| + | [[Category: Tight junction]] | ||
Revision as of 10:24, 10 September 2017
Crystal structure of the coiled-coil domain of human tricellulin
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