8S1M
Crystal structure of human GABARAP fused to EGFR (1076-1099)
Summary for 8S1M
| Entry DOI | 10.2210/pdb8s1m/pdb |
| Descriptor | Epidermal growth factor receptor,Gamma-aminobutyric acid receptor-associated protein, CHLORIDE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | atg8, receptor-trafficking, protein binding |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 1 |
| Total formula weight | 17032.79 |
| Authors | Ueffing, A.,Willbold, D.,Weiergraeber, O.H. (deposition date: 2024-02-15, release date: 2024-08-14, Last modification date: 2025-01-15) |
| Primary citation | Uffing, A.,Weiergraber, O.H.,Schwarten, M.,Hoffmann, S.,Willbold, D. GABARAP interacts with EGFR - supporting the unique role of this hAtg8 protein during receptor trafficking. Febs Lett., 598:2656-2669, 2024 Cited by PubMed Abstract: The human Atg8 family member GABARAP is involved in numerous autophagy-related and -unrelated processes. We recently observed that specifically the deficiency of GABARAP enhances epidermal growth factor receptor (EGFR) degradation upon ligand stimulation. Here, we report on two putative LC3-interacting regions (LIRs) within EGFR, the first of which (LIR1) is selected as a GABARAP binding site in silico. Indeed, in vitro interaction studies reveal preferential binding of LIR1 to GABARAP and GABARAPL1. Our X-ray data demonstrate interaction of core LIR1 residues FLPV with both hydrophobic pockets of GABARAP suggesting canonical binding. Although LIR1 occupies the LIR docking site, GABARAP Y49 and L50 appear dispensable in this case. Our data support the hypothesis that GABARAP affects the fate of EGFR at least in part through direct binding. PubMed: 39160442DOI: 10.1002/1873-3468.14997 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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