3DOW

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

3DOW の概要

• エントリーDOI: 10.2210/pdb3dow/pdb
• 関連するPDBエントリー: 3D32
• 分子名称: Gamma-aminobutyric acid receptor-associated protein, CRT peptide, ZINC ION, ... (4 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Endomembrane system (By similarity): O95166; Endoplasmic reticulum lumen: P27797
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15482.99

構造登録者

Thielmann, Y.,Weiergraeber, O.H.,Willbold, D. (登録日: 2008-07-07, 公開日: 2009-02-24, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)