1xaw: Difference between revisions
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'''crystal structure of the cytoplasmic distal C-terminal domain of occludin''' | {{Structure | ||
|PDB= 1xaw |SIZE=350|CAPTION= <scene name='initialview01'>1xaw</scene>, resolution 1.45Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= OCLN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''crystal structure of the cytoplasmic distal C-terminal domain of occludin''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1XAW is a [ | 1XAW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAW OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16081103 16081103] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:07:21 2008'' | ||
Revision as of 13:07, 20 March 2008
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| 1xaw, resolution 1.45Å | |||||||||||||
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| Gene: | OCLN (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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