1wpa

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpa OCA], [http://www.ebi.ac.uk/pdbsum/1wpa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wpa RCSB]</span>
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[[Category: zo-1 binding]]
[[Category: zo-1 binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:39:18 2008''

Revision as of 21:39, 30 March 2008


PDB ID 1wpa

Drag the structure with the mouse to rotate
, resolution 1.5Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



1.5 Angstrom crystal structure of human occludin fragment 413-522


Overview

Occludin is a transmembrane protein localized at tight junctions whose functions are complex yet poorly understood. Current evidence supports a role for occludin in both the formation of the paracellular barrier and in cell signaling. While the N-terminal extracellular domains of occludin mediate homotypic adhesion, the distal C-terminal cytoplasmic domain of occludin controls protein targeting and endocytosis. The C terminus can also bind to the scaffolding proteins ZO-1, ZO-2, ZO-3, cingulin, the membrane trafficking protein VAP33, and the cytoskeletal protein F-actin, suggesting an important role for this domain. This domain is highly homologous to an important functional domain in the C terminus of the ELL family of RNA polymerase II transcription factors. To explore the function of occludin, we determined the high-resolution crystal structure of its C-terminal distal cytoplasmic domain. The structure comprises three helices that form two separate anti-parallel coiled-coils and a loop that packs tightly against one of the coiled-coils. Using in vitro binding studies and site-directed mutagenesis, we have identified a large positively charged surface that contains the binding site for ZO-1, and this surface is required for proper localization of occludin to cell-cell junctions. On the basis of sequence conservation, we predict that occludin domains from different species and the C-terminal domain of the ELL transcription factors share a very similar structure. Our results provide a model to further test the function of occludin and its binding to other proteins.

About this Structure

1WPA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the conserved cytoplasmic C-terminal domain of occludin: identification of the ZO-1 binding surface., Li Y, Fanning AS, Anderson JM, Lavie A, J Mol Biol. 2005 Sep 9;352(1):151-64. PMID:16081103

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