Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8.
Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the detailed molecular basis of the interaction between these two receptors remains to be elucidated. Here, we report the biochemical characterization of ... both NDP52 and galectin-8 as well as the crystal structure of galectin-8 complexed with an NDP52 peptide. The unexpected observation of nicotinamide adenine dinucleotide located at the carbohydrate-binding site expands our knowledge of the sugar-binding specificity of galectin-8. The NDP52-galectin-8 complex structure explains the key determinants for recognition on both receptors and defines a special orientation of N- and C-terminal carbohydrate recognition domains of galectin-8. Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules. These results lay the groundwork for understanding how host cells target bacterial pathogens for autophagy.
Mesh Terms:
Amino Acid Sequence, Autophagy, Crystallography, X-Ray, Dimerization, Electrophoresis, Polyacrylamide Gel, Galectins, Humans, Models, Molecular, Molecular Sequence Data, Mutagenesis, NAD, Nuclear Proteins, Protein Binding, Protein Conformation, Sequence Homology, Amino Acid
Amino Acid Sequence, Autophagy, Crystallography, X-Ray, Dimerization, Electrophoresis, Polyacrylamide Gel, Galectins, Humans, Models, Molecular, Molecular Sequence Data, Mutagenesis, NAD, Nuclear Proteins, Protein Binding, Protein Conformation, Sequence Homology, Amino Acid
Nat Commun
Date: Mar. 21, 2013
PubMed ID: 23511477
View in: Pubmed Google Scholar
Download Curated Data For This Publication
166314
Switch View:
- Interactions 3