4HAN

Crystal structure of Galectin 8 with NDP52 peptide

Summary for 4HAN

• Entry DOI: 10.2210/pdb4han/pdb
• Descriptor: Galectin-8, Calcium-binding and coiled-coil domain-containing protein 2, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: autophagy, innate immunity, carbohydrate recognition domain (crd), autophagy adapter molecule, nad binding, ndp52 peoptide binding, cytosol, sugar binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasmic vesicle : O00214; Cytoplasm, perinuclear region : Q13137
• Total number of polymer chains: 4
• Total formula weight: 71020.75

Authors

Kim, B.-W.,Hong, S.B.,Kim, J.H.,Kwon, D.H.,Song, H.K. (deposition date: 2012-09-27, release date: 2013-03-20, Last modification date: 2024-02-28)

Primary citation

Kim, B.W.,Hong, S.B.,Kim, J.H.,Kwon, D.H.,Song, H.K.
Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8.
Nat Commun, 4:1613-1613, 2013

PubMed Abstract: 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.

PubMed: 23511477
DOI: 10.1038/ncomms2606

Experimental method

X-RAY DIFFRACTION (2.551 Å)