2gd5: Difference between revisions

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{{STRUCTURE_2gd5|  PDB=2gd5  |  SCENE=  }}  
{{STRUCTURE_2gd5|  PDB=2gd5  |  SCENE=  }}  


'''Structural basis for budding by the ESCRTIII factor CHMP3'''
===Structural basis for budding by the ESCRTIII factor CHMP3===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Chmp3]]
[[Category: Chmp3]]
[[Category: Escrt-iii]]
[[Category: Escrt-iii]]
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Revision as of 20:43, 28 July 2008

File:2gd5.png

Template:STRUCTURE 2gd5

Structural basis for budding by the ESCRTIII factor CHMP3

Template:ABSTRACT PUBMED 16740483

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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