Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8
- Authors
- Kim, Byeong-Won; Hong, Seung Beom; Kim, Jun Hoe; Kwon, Do Hoon; Song, Hyun Kyu
- Issue Date
- 3월-2013
- Publisher
- NATURE PUBLISHING GROUP
- Citation
- NATURE COMMUNICATIONS, v.4
- Indexed
- SCIE
SCOPUS
- Journal Title
- NATURE COMMUNICATIONS
- Volume
- 4
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/103861
- DOI
- 10.1038/ncomms2606
- ISSN
- 2041-1723
- 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Graduate School > Department of Life Sciences > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholar.korea.ac.kr/handle/2021.sw.korea/103861)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.