1uru

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{{STRUCTURE_1uru| PDB=1uru | SCENE= }}
{{STRUCTURE_1uru| PDB=1uru | SCENE= }}
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'''AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA'''
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===AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Endocytosis]]
[[Category: Endocytosis]]
[[Category: Membrane curvature]]
[[Category: Membrane curvature]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:36:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:51:42 2008''

Revision as of 06:51, 28 July 2008

Image:1uru.png

Template:STRUCTURE 1uru

AMPHIPHYSIN BAR DOMAIN FROM DROSOPHILA

Template:ABSTRACT PUBMED 14645856

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

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