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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zhao Y,Ren J,Harlos K,Stuart DIdoi
10.1002/1873-3468.12089subject
Has Abstractpub_date
2016-03-01 00:00:00pages
605-12issue
5eissn
0014-5793issn
1873-3468journal_volume
590pub_type
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