Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2016 May 26;165(6):1467–1478. doi: 10.1016/j.cell.2016.05.022

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2016 Elsevier Inc.

Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

PMC Copyright notice

Structure of the Transmembrane Domain TMD of hNPC1

(A) TMs 2–13 of hNPC1 exhibit a characteristic resistance-nodulation-cell division superfamily fold. The two repeats in the RND fold are colored cyan and light purple, respectively. The invisible cytoplasmic segments are shown as dotted lines. The arrows in the left panel indicate the N→C orientation of the corresponding TMs. Right panel: TMs 2–7 are related to TMs 8–13 by a 180-degree rotation around an axis that is perpendicular to the membrane plane.

(B) The sterol sensing domain (SSD). TMs 3–7 of hNPC1 constitute the SSD that is also found in several proteins involved in sterol metabolism or signaling. Two perpendicular side views are shown.

(C) Structural similarity between the TMDs of hNPC1 and the bacterial multidrug efflux transporter AcrB. Right panel: the SSD-corresponding TMs in AcrB are exposed to the lipid bilayer in the context of trimer (PDB: 1IWG).