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5n7k

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Current revision

Crystal structure of the coiled-coil domain of human tricellulin

Structural highlights

5n7k is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.81Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MALD2_HUMAN Autosomal recessive non-syndromic sensorineural deafness type DFNB. The disease is caused by mutations affecting the gene represented in this entry.

Function

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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Riazuddin S, Ahmed ZM, Fanning AS, Lagziel A, Kitajiri S, Ramzan K, Khan SN, Chattaraj P, Friedman PL, Anderson JM, Belyantseva IA, Forge A, Riazuddin S, Friedman TB. Tricellulin is a tight-junction protein necessary for hearing. Am J Hum Genet. 2006 Dec;79(6):1040-51. Epub 2006 Oct 31. PMID:17186462 doi:http://dx.doi.org/10.1086/510022
↑ Schuetz A, Radusheva V, Krug SM, Heinemann U. Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization. Ann N Y Acad Sci. 2017 Jun 29. doi: 10.1111/nyas.13408. PMID:28661558 doi:http://dx.doi.org/10.1111/nyas.13408

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5n7k"

Categories: Homo sapiens | Large Structures | Heinemann U | Schuetz A

@@ Line 3: / Line 3: @@
 <StructureSection load='5n7k' size='340' side='right'caption='[[5n7k]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5n7k]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N7K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5N7K FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5n7k]] is a 4 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=5N7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N7K FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5n7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n7k OCA], [http://pdbe.org/5n7k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n7k RCSB], [http://www.ebi.ac.uk/pdbsum/5n7k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n7k ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.81&#8491;</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=5n7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n7k OCA], [https://pdbe.org/5n7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n7k RCSB], [https://www.ebi.ac.uk/pdbsum/5n7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n7k 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.
+[https://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>
+[https://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 ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Heinemann, U]]
+[[Category: Heinemann U]]
-[[Category: Schuetz, A]]
+[[Category: Schuetz A]]
-[[Category: Cc domain]]
-[[Category: Cell adhesion]]
-[[Category: Dimerization]]
-[[Category: Tight junction]]

5n7k

From Proteopedia

Current revision

Crystal structure of the coiled-coil domain of human tricellulin

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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