2gd5
From Proteopedia
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| - | [[Image:2gd5.gif|left|200px]] | + | [[Image:2gd5.gif|left|200px]] |
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| - | '''Structural basis for budding by the ESCRTIII factor CHMP3''' | + | {{Structure |
| + | |PDB= 2gd5 |SIZE=350|CAPTION= <scene name='initialview01'>2gd5</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CHMP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Structural basis for budding by the ESCRTIII factor CHMP3''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GD5 is a [ | + | 2GD5 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=2GD5 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16740483 16740483] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: escrt-iii]] | [[Category: escrt-iii]] | ||
| - | ''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 17:03:20 2008'' |
Revision as of 15:03, 20 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | CHMP3 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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