1x03
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(New page: 200px<br /> <applet load="1x03" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x03, resolution 3.1Å" /> '''Crystal structure of...)
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Revision as of 17:50, 12 November 2007
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Crystal structure of endophilin BAR domain
Overview
The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a, versatile protein module that senses and generates positive membrane, curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 A, has a unique structure consisting of a pair of helix-loop appendages, sprouting out from the crescent. The appendage's short helices form a, hydrophobic ridge, which runs across the concave surface at its center., Examining liposome binding and tubulation in vitro using purified BAR, domain and its mutants indicated that the ridge penetrates into the, membrane bilayer and enhances liposome tubulation. BAR domain-expressing, cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a, swinging-arm mutant lost liposome tubulation activity yet retaining, liposome binding. These data suggested that the rigid crescent dimer shape, is crucial for the tubulation. We here propose that the BAR domain drives, membrane curvature by coordinate action of the crescent's scaffold, mechanism and the ridge's membrane insertion in addition to membrane, binding via amino-terminal amphipathic helix.
About this Structure
1X03 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms., Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, Mochizuki N, EMBO J. 2006 Jun 21;25(12):2889-97. Epub 2006 Jun 8. PMID:16763557
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