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Publication Abstract from PubMed

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.

Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8.,Kim BW, Hong SB, Kim JH, Kwon do H, Song HK Nat Commun. 2013;4:1613. doi: 10.1038/ncomms2606. PMID:23511477^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.