4HAN

Crystal structure of Galectin 8 with NDP52 peptide

4HAN の概要

• エントリーDOI: 10.2210/pdb4han/pdb
• 分子名称: Galectin-8, Calcium-binding and coiled-coil domain-containing protein 2, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: autophagy, innate immunity, carbohydrate recognition domain (crd), autophagy adapter molecule, nad binding, ndp52 peoptide binding, cytosol, sugar binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasmic vesicle : O00214; Cytoplasm, perinuclear region : Q13137
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 71020.75

構造登録者

Kim, B.-W.,Hong, S.B.,Kim, J.H.,Kwon, D.H.,Song, H.K. (登録日: 2012-09-27, 公開日: 2013-03-20, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.551 Å)