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| - | [[Image:1wpa.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1wpa| PDB=1wpa | SCENE= }} | | {{STRUCTURE_1wpa| PDB=1wpa | SCENE= }} |
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| - | '''1.5 Angstrom crystal structure of human occludin fragment 413-522'''
| + | ===1.5 Angstrom crystal structure of human occludin fragment 413-522=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16081103}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16081103 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16081103}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Transmembrane protein]] | | [[Category: Transmembrane protein]] |
| | [[Category: Zo-1 binding]] | | [[Category: Zo-1 binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:58:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:04:01 2008'' |
Revision as of 11:04, 27 July 2008
Template:STRUCTURE 1wpa
1.5 Angstrom crystal structure of human occludin fragment 413-522
Template:ABSTRACT PUBMED 16081103
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
Page seeded by OCA on Sun Jul 27 14:04:01 2008
