Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones.

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Citation

Thielmann Y, Weiergraber OH, Mohrluder J, Willbold D

Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones.

FEBS J. 2009 Feb;276(4):1140-52. doi: 10.1111/j.1742-4658.2008.06857.x. Epub 2009 Jan 16.

PubMed ID
19154346 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
CalreticulinP27797Details