3DOW

Complex structure of GABA type A receptor associated protein and its binding epitope on calreticulin

Summary for 3DOW

• Entry DOI: 10.2210/pdb3dow/pdb
• Related: 3D32
• Descriptor: Gamma-aminobutyric acid receptor-associated protein, CRT peptide, ZINC ION, ... (4 entities in total)
• Functional Keywords: alpha-beta, beta-grasp fold, cytoplasm, cytoskeleton, golgi apparatus, membrane, microtubule, protein transport, transport, calcium, chaperone, endoplasmic reticulum, extracellular matrix, lectin, metal-binding, secreted, zinc
• Biological source: Homo sapiens; More
• Cellular location: Endomembrane system (By similarity): O95166; Endoplasmic reticulum lumen: P27797
• Total number of polymer chains: 2
• Total formula weight: 15482.99

Authors

Thielmann, Y.,Weiergraeber, O.H.,Willbold, D. (deposition date: 2008-07-07, release date: 2009-02-24, Last modification date: 2024-10-30)

Primary citation

Thielmann, Y.,Weiergraber, O.H.,Mohrluder, J.,Willbold, D.
Structural framework of the GABARAP-calreticulin interface - implications for substrate binding to endoplasmic reticulum chaperones.
Febs J., 276:1140-1152, 2009

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.

PubMed: 19154346
DOI: 10.1111/j.1742-4658.2008.06857.x

Experimental method

X-RAY DIFFRACTION (2.3 Å)