Title : Structure of glycosylated
NPC1 luminal domain C reveals insights into
NPC2 and Ebola virus interactions
Abstract :
- 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 seven possible sites are glycosylated
- Mapping the disease mutations onto the glycosylated structure reveals a potential binding face for NPC2
- Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues , H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. glycosylated, , -, all seven possible sites, -
- 4. glycoprotein, , glycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):