Sterical Hindrance Promotes Selectivity of the Autophagy Cargo Receptor NDP52 for the Danger Receptor Galectin-8 in Antibacterial Autophagy
Copyright policy )Sterical Hindrance Promotes Selectivity of the Autophagy Cargo Receptor NDP52 for the Danger Receptor Galectin-8 in Antibacterial Autophagy
A crystal structure of an autophagy receptor with a ligand reveals how Salmonella is specifically targeted for degradation.
- University of Science and Technology of China China (People's Republic of)
- Medical Research Council United Kingdom
- MRC Laboratory of Molecular Biology United Kingdom
Models, Molecular, Binding Sites, Microscopy, Confocal, Galectins, Molecular Sequence Data, Nuclear Proteins, Hydrogen Bonding, Endosomes, Intracellular Membranes, Protein Structure, Tertiary, Cytosol, Host-Pathogen Interactions, Mutation, Autophagy, Humans, Amino Acid Sequence, Lysosomes, Hydrophobic and Hydrophilic Interactions, HeLa Cells, Protein Binding
Models, Molecular, Binding Sites, Microscopy, Confocal, Galectins, Molecular Sequence Data, Nuclear Proteins, Hydrogen Bonding, Endosomes, Intracellular Membranes, Protein Structure, Tertiary, Cytosol, Host-Pathogen Interactions, Mutation, Autophagy, Humans, Amino Acid Sequence, Lysosomes, Hydrophobic and Hydrophilic Interactions, HeLa Cells, Protein Binding
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