English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structure of the mitochondrial translocator protein in complex with a diagnostic ligand.

Jaremko, L., Jaremko, M., Giller, K., Becker, S., & Zweckstetter, M. (2014). Structure of the mitochondrial translocator protein in complex with a diagnostic ligand. Science, 343(6177), 1363-1366. doi:10.1126/science.1248725.

Item is

Files

show Files
hide Files
:
2008012.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
2008012.pdf
Description:
-
OA-Status:
Visibility:
Restricted (UNKNOWN id 303; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
2008012_Suppl.pdf (Supplementary material), 2MB
Name:
2008012_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
OA-Status:

Creators

show
hide
 Creators:
Jaremko, L.1, Author           
Jaremko, M.1, Author           
Giller, K.1, Author           
Becker, S.1, Author           
Zweckstetter, M.2, Author           
Affiliations:
1Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_578567              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

Content

show
hide
Free keywords: -
 Abstract: The 18-kilodalton translocator protein TSPO is found in mitochondrial membranes and mediates the import of cholesterol and porphyrins into mitochondria. In line with the role of TSPO in mitochondrial function, TSPO ligands are used for a variety of diagnostic and therapeutic applications in animals and humans. We present the three-dimensional high-resolution structure of mammalian TSPO reconstituted in detergent micelles in complex with its high-affinity ligand PK11195. The TSPO-PK11195 structure is described by a tight bundle of five transmembrane alpha helices that form a hydrophobic pocket accepting PK11195. Ligand-induced stabilization of the structure of TSPO suggests a molecular mechanism for the stimulation of cholesterol transport into mitochondria.

Details

show
hide
Language(s): eng - English
 Dates: 2014-03-21
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.1248725
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Science
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 343 (6177) Sequence Number: - Start / End Page: 1363 - 1366 Identifier: -