2gd5
From Proteopedia
(New page: 200px<br /> <applet load="2gd5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gd5, resolution 2.80Å" /> '''Structural basis fo...) |
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| - | [[Image:2gd5.gif|left|200px]]<br /> | + | [[Image:2gd5.gif|left|200px]]<br /><applet load="2gd5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2gd5" size=" | + | |
caption="2gd5, resolution 2.80Å" /> | caption="2gd5, resolution 2.80Å" /> | ||
'''Structural basis for budding by the ESCRTIII factor CHMP3'''<br /> | '''Structural basis for budding by the ESCRTIII factor CHMP3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The vacuolar protein sorting machinery regulates multivesicular body | + | The vacuolar protein sorting machinery regulates multivesicular body biogenesis and is selectively recruited by enveloped viruses to support budding. Here we report the crystal structure of the human ESCRT-III protein CHMP3 at 2.8 A resolution. The core structure of CHMP3 folds into a flat helical arrangement that assembles into a lattice, mainly via two different dimerization modes, and unilaterally exposes a highly basic surface. The C terminus, the target for Vps4-induced ESCRT disassembly, extends from the opposite side of the membrane targeting region. Mutations within the basic and dimerization regions hinder bilayer interaction in vivo and reverse the dominant-negative effect of a truncated CHMP3 fusion protein on HIV-1 budding. Thus, the final steps in the budding process may include CHMP protein polymerization and lattice formation on membranes by employing different bilayer-recognizing surfaces, a function shared by all CHMP family members. |
==About this Structure== | ==About this Structure== | ||
| - | 2GD5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2GD5 is a [http://en.wikipedia.org/wiki/Single_protein 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=2GD5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gottlinger, H.]] | [[Category: Gottlinger, H.]] | ||
| - | [[Category: Muziol, T | + | [[Category: Muziol, T M.]] |
[[Category: Pineda-Molina, E.]] | [[Category: Pineda-Molina, E.]] | ||
| - | [[Category: Ravelli, R | + | [[Category: Ravelli, R B.]] |
[[Category: Usami, Y.]] | [[Category: Usami, Y.]] | ||
[[Category: Weissenhorn, W.]] | [[Category: Weissenhorn, W.]] | ||
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[[Category: escrt-iii]] | [[Category: escrt-iii]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:33 2008'' |
Revision as of 15:30, 21 February 2008
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Structural basis for budding by the ESCRTIII factor CHMP3
Overview
The vacuolar protein sorting machinery regulates multivesicular body biogenesis and is selectively recruited by enveloped viruses to support budding. Here we report the crystal structure of the human ESCRT-III protein CHMP3 at 2.8 A resolution. The core structure of CHMP3 folds into a flat helical arrangement that assembles into a lattice, mainly via two different dimerization modes, and unilaterally exposes a highly basic surface. The C terminus, the target for Vps4-induced ESCRT disassembly, extends from the opposite side of the membrane targeting region. Mutations within the basic and dimerization regions hinder bilayer interaction in vivo and reverse the dominant-negative effect of a truncated CHMP3 fusion protein on HIV-1 budding. Thus, the final steps in the budding process may include CHMP protein polymerization and lattice formation on membranes by employing different bilayer-recognizing surfaces, a function shared by all CHMP family members.
About this Structure
2GD5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for budding by the ESCRT-III factor CHMP3., Muziol T, Pineda-Molina E, Ravelli RB, Zamborlini A, Usami Y, Gottlinger H, Weissenhorn W, Dev Cell. 2006 Jun;10(6):821-30. PMID:16740483
Page seeded by OCA on Thu Feb 21 17:30:33 2008
