Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses. We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all...
Główni autorzy: | Zhao, Y, Ren, J, Harlos, K, Stuart, D |
---|---|
Format: | Journal article |
Język: | English |
Wydane: |
Wiley
2016
|
Podobne zapisy
-
Inter-domain dynamics drive cholesterol transport by NPC1 and NPC1L1 proteins
od: Piyali Saha, i wsp.
Wydane: (2020-05-01) -
The NPC pathway and persistence of intracellular pathogens
od: Weng, Y
Wydane: (2023) -
MemoryRepository for AI NPC
od: Shijie Zheng, i wsp.
Wydane: (2024-01-01) -
Pulmonary abnormalities in animal models due to Niemann-Pick type C1 (NPC1) or C2 (NPC2) disease.
od: Blair R Roszell, i wsp.
Wydane: (2013-01-01) -
Utility of primary cells to examine NPC1 receptor expression in Mops condylurus, a potential Ebola virus reservoir.
od: Marcel Bokelmann, i wsp.
Wydane: (2020-01-01)