2d4c
From Proteopedia
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| - | [[Image:2d4c.gif|left|200px]] | + | [[Image:2d4c.gif|left|200px]] |
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| - | '''Crystal structure of the endophilin BAR domain mutant''' | + | {{Structure |
| + | |PDB= 2d4c |SIZE=350|CAPTION= <scene name='initialview01'>2d4c</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of the endophilin BAR domain mutant''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2D4C is a [ | + | 2D4C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D4C OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16763557 16763557] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: bar domain]] | [[Category: bar domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:23:09 2008'' |
Revision as of 14:23, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the endophilin BAR domain mutant
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
2D4C 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
Page seeded by OCA on Thu Mar 20 16:23:09 2008
Categories: Homo sapiens | Single protein | Masuda, M. | Takeda, S. | CA | Bar domain
