Crystal structures of translocator protein (TSPO) and mutant mimic of a human polymorphism

Author:

Li Fei1,Liu Jian1,Zheng Yi1,Garavito R. Michael1,Ferguson-Miller Shelagh1

Affiliation:

1. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.

Abstract

Structural clues to protein function Translocator protein (TSPO) is a mitochondrial membrane protein thought to transport cholesterol and porphyrins. Its detailed function remains unclear, but interest in it is high because TSPO is involved in a variety of human diseases. Two papers now present crystal structures of bacterial TSPOs. Li et al. show that a mutant that mimics a human single polymorphism associated with psychiatric disorders has structural changes in a region implicated in cholesterol binding. Guo et al. suggest that TSPO may be more than a transporter. They show how it catalyzes the degradation of porphyrins, a function that could be important in protection against oxidative stress. Science , this issue p. 555 , p. 551

Funder

NIH

National Cancer Institute

National Institute of General Medical Sciences

Michigan State University Strategic Partnership Grant

Mitochondrial Science and Medicine

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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