Journal
FEBS JOURNAL
Volume 276, Issue 4, Pages 1140-1152Publisher
WILEY
DOI: 10.1111/j.1742-4658.2008.06857.x
Keywords
4-aminobutyrate type A receptor-associated protein (GABARAP); calreticulin; protein-protein interaction; structure model; X-ray crystallography
Categories
Funding
- Deutsche Forschungsgemeinschaft (DFG) [Wi1472/5]
Ask authors/readers for more resources
The 4-aminobutyrate type A receptor-associated protein (GABARAP) is a versatile adaptor protein that plays an important role in intracellular vesicle trafficking, particularly in neuronal cells. We have investigated the structural determinants underlying the interaction of GABARAP with calreticulin using spectroscopic and crystallographic techniques. Specifically, we present the crystal structure of GABARAP in complex with its major binding epitope on the chaperone. Molecular modeling of a complex containing full-length calreticulin suggests a novel mode of substrate interaction, which may have functional implications for the calreticulin/calnexin family in general.
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