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Journal article

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 glyc...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1002/1873-3468.12089

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author
More from this funder
Funding agency for:
Zhao, Y
Grant:
FP7/2007-2013) Grant Biostruct-X project (283570
More from this funder
Funding agency for:
Ren, J
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Funding agency for:
Harlos, K
Grant:
(FP7/2007-2013) Grant Biostruct-X project (283570)
More from this funder
Funding agency for:
Stuart, D
Grant:
MR/N00065X/1
Publisher:
Wiley Publisher's website
Journal:
FEBS Letters Journal website
Volume:
590
Issue:
5
Pages:
605-612
Publication date:
2016-02-23
Acceptance date:
2016-01-28
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
Source identifiers:
601474
Language:
English
Keywords:
Pubs id:
pubs:601474
UUID:
uuid:3af02f4c-370c-4a0b-b3d2-f43c6161b0c6
Local pid:
pubs:601474
Deposit date:
2016-05-20

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