Journal
CELL
Volume 125, Issue 1, Pages 113-126Publisher
CELL PRESS
DOI: 10.1016/j.cell.2006.01.049
Keywords
-
Categories
Funding
- NIDDK NIH HHS [Z01 DK036118-12] Funding Source: Medline
Ask authors/readers for more resources
The endosomal sorting complex required for transport (ESCRT) complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. The yeast ESCRT-I complex contains the Vps23, Vps28, and Vps37 proteins, and its assembly is directed by the C-terminal steadiness box of Vps23, the N-terminal half of Vps28, and the C-terminal half of Vps37. The crystal structures of a Vps23:Vps28 core sub-complex and the Vps23:Vps28:Vps37 core were solved at 2.1 and 2.8 angstrom resolution. Each subunit contains a structurally similar pair of helices that form the core. The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic. The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available