View source for 1uru

[[Image:1uru.gif|left|200px]]<br /><applet load="1uru" size="450" 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.

==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]. 

==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14645856 14645856]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Evans, P.R.]]
[[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''