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4p79

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Revision as of 16:17, 4 August 2016

Crystal structure of mouse claudin-15

Structural highlights

4p79 is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:	Cldn15 (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CLD15_MOUSE] Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity (By similarity).

Publication Abstract from PubMed

Tight junctions are cell-cell adhesion structures in epithelial cell sheets that surround organ compartments in multicellular organisms and regulate the permeation of ions through the intercellular space. Claudins are the major constituents of tight junctions and form strands that mediate cell adhesion and function as paracellular barriers. We report the structure of mammalian claudin-15 at a resolution of 2.4 angstroms. The structure reveals a characteristic beta-sheet fold comprising two extracellular segments, which is anchored to a transmembrane four-helix bundle by a consensus motif. Our analyses suggest potential paracellular pathways with distinctive charges on the extracellular surface, providing insight into the molecular basis of ion homeostasis across tight junctions.

Crystal structure of a claudin provides insight into the architecture of tight junctions.,Suzuki H, Nishizawa T, Tani K, Yamazaki Y, Tamura A, Ishitani R, Dohmae N, Tsukita S, Nureki O, Fujiyoshi Y Science. 2014 Apr 18;344(6181):304-7. doi: 10.1126/science.1248571. PMID:24744376^[1]

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

References

↑ Suzuki H, Nishizawa T, Tani K, Yamazaki Y, Tamura A, Ishitani R, Dohmae N, Tsukita S, Nureki O, Fujiyoshi Y. Crystal structure of a claudin provides insight into the architecture of tight junctions. Science. 2014 Apr 18;344(6181):304-7. doi: 10.1126/science.1248571. PMID:24744376 doi:http://dx.doi.org/10.1126/science.1248571

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4p79"

@@ Line 1: / Line 1: @@
 ==Crystal structure of mouse claudin-15==
 <StructureSection load='4p79' size='340' side='right' caption='[[4p79]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cldn15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4p79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p79 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p79 RCSB], [http://www.ebi.ac.uk/pdbsum/4p79 PDBsum]</span></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=4p79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p79 OCA], [http://pdbe.org/4p79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p79 RCSB], [http://www.ebi.ac.uk/pdbsum/4p79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p79 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4p79" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4p79

From Proteopedia

Revision as of 16:17, 4 August 2016

Crystal structure of mouse claudin-15

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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