2gd5 | pdb_00002gd5
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 Mon Nov 12 22:17:31 2007
