1xaw

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[[Image:1xaw.gif|left|200px]]
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{{Structure
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|GENE= OCLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xaw OCA], [http://www.ebi.ac.uk/pdbsum/1xaw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xaw RCSB]</span>
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'''crystal structure of the cytoplasmic distal C-terminal domain of occludin'''
'''crystal structure of the cytoplasmic distal C-terminal domain of occludin'''
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[[Category: Lavie, A.]]
[[Category: Lavie, A.]]
[[Category: Li, Y.]]
[[Category: Li, Y.]]
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[[Category: coiled-coil]]
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[[Category: Coiled-coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:47:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:47:06 2008''
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Revision as of 11:47, 3 May 2008

Template:STRUCTURE 1xaw

crystal structure of the cytoplasmic distal C-terminal domain of occludin


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

1XAW 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 Page seeded by OCA on Sat May 3 14:47:54 2008

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