1xaw: Difference between revisions

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[[Image:1xaw.gif|left|200px]]<br />

[[Image:1xaw.gif|left|200px]]<br /><applet load="1xaw" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1xaw" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1xaw, resolution 1.45Å" />

'''crystal structure of the cytoplasmic distal C-terminal domain of occludin'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1XAW OCA].

1XAW is a [http://en.wikipedia.org/wiki/Single_protein 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==

Line 14:

Line 13:

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Anderson, J.M.]]

[[Category: Anderson, J M.]]

[[Category: Fanning, A.S.]]

[[Category: Fanning, A S.]]

[[Category: Lavie, A.]]

[[Category: Li, Y.]]

[[Category: coiled-coil]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:02:~~54 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:52 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1xaw.gif|left|200px]]<br />
+[[Image:1xaw.gif|left|200px]]<br /><applet load="1xaw" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1xaw" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1xaw, resolution 1.45&Aring;" />
 '''crystal structure of the cytoplasmic distal C-terminal domain of occludin'''<br />
 ==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.
+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==
-XAW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XAW OCA].
+XAW is a [http://en.wikipedia.org/wiki/Single_protein 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==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Anderson, J.M.]]
+[[Category: Anderson, J M.]]
-[[Category: Fanning, A.S.]]
+[[Category: Fanning, A S.]]
 [[Category: Lavie, A.]]
 [[Category: Li, Y.]]
 [[Category: coiled-coil]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:02:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:52 2008''