1uru
From Proteopedia
(New page: 200px<br /><applet load="1uru" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uru, resolution 2.60Å" /> '''AMPHIPHYSIN BAR DOMA...) |
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| - | [[Image:1uru.gif|left|200px]]<br /><applet load="1uru" size=" | + | [[Image:1uru.gif|left|200px]]<br /><applet load="1uru" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uru, resolution 2.60Å" /> | caption="1uru, resolution 2.60Å" /> | ||
'''AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA'''<br /> | '''AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Evans, P | + | [[Category: Evans, P R.]] |
| - | [[Category: Kent, H | + | [[Category: Kent, H M.]] |
[[Category: coiled-coil]] | [[Category: coiled-coil]] | ||
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
[[Category: membrane curvature]] | [[Category: membrane curvature]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:39 2008'' |
Revision as of 13:27, 21 February 2008
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AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA
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.
About this Structure
1URU is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
BAR domains as sensors of membrane curvature: the amphiphysin BAR structure., Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT, Science. 2004 Jan 23;303(5657):495-9. Epub 2003 Nov 26. PMID:14645856
Page seeded by OCA on Thu Feb 21 15:27:39 2008
