1uru: Difference between revisions

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[[Image:1uru.gif|left|200px]]<br /><applet load="1uru" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

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

caption="1uru, resolution 2.60Å" />

'''AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA'''<br />

==Overview==

The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in, amphiphysins from yeast to human and is also found in endophilins and, nadrins. We solved the structure of the Drosophila amphiphysin BAR domain., It is a crescent-shaped dimer that binds preferentially to highly curved, negatively charged membranes. With its N-terminal amphipathic helix and, BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and, in vivo. The structure is similar to that of arfaptin2, which we find also, binds and tubulates membranes. From this, we predict that BAR domains are, in many protein families, including sorting nexins, centaurins, and, oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.

The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.

==About this Structure==

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

1URU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URU OCA].

==Reference==

Line 13:

[[Category: Drosophila melanogaster]]

[[Category: Single protein]]

[[Category: Evans, P.R.]]

[[Category: Evans, P R.]]

[[Category: Kent, H.M.]]

[[Category: Kent, H M.]]

[[Category: coiled-coil]]

[[Category: endocytosis]]

[[Category: membrane curvature]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 25 04~~:20:~~33 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:39 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1uru.gif|left|200px]]<br /><applet load="1uru" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1uru.gif|left|200px]]<br /><applet load="1uru" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1uru, resolution 2.60&Aring;" />
 '''AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA'''<br />
 ==Overview==
-The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in, amphiphysins from yeast to human and is also found in endophilins and, nadrins. We solved the structure of the Drosophila amphiphysin BAR domain., It is a crescent-shaped dimer that binds preferentially to highly curved, negatively charged membranes. With its N-terminal amphipathic helix and, BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and, in vivo. The structure is similar to that of arfaptin2, which we find also, binds and tubulates membranes. From this, we predict that BAR domains are, in many protein families, including sorting nexins, centaurins, and, oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
+The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
 ==About this Structure==
-URU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1URU OCA].
+URU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1URU OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Drosophila melanogaster]]
 [[Category: Single protein]]
-[[Category: Evans, P.R.]]
+[[Category: Evans, P R.]]
-[[Category: Kent, H.M.]]
+[[Category: Kent, H M.]]
 [[Category: coiled-coil]]
 [[Category: endocytosis]]
 [[Category: membrane curvature]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:20:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:39 2008''