%0 Journal Article %1 Li2015TSPOCrystal %A Li, Fei %A Liu, Jian %A Garavito, R. Michael %A Ferguson-Miller, Shelagh %D 2015 %J Pharmacological Research %K TSPO crystallography %P 404 - 409 %R http://dx.doi.org/10.1016/j.phrs.2015.03.022 %T Evolving understanding of translocator protein 18 kDa (TSPO) %U http://www.sciencedirect.com/science/article/pii/S1043661815000626 %V 99 %X Abstract The translocator protein 18 kDa (TSPO) has been the focus of intense research by the biomedical community and the pharmaceutical industry because of its apparent involvement in many disease-related processes. These include steroidogenesis, apoptosis, inflammation, neurological disease and cancer, resulting in the use of \TSPO\ as a biomarker and its potential as a drug target. Despite more than 30 years of study, the precise function of \TSPO\ remains elusive. A recent breakthrough in determining the high-resolution crystal structures of bacterial homologs of mitochondrial \TSPO\ provides new insight into the structural and functional properties at a molecular level and new opportunities for investigating the significance of this ancient and highly conserved protein family. The availability of atomic level structural information from different species also provides a platform for structure-based drug development. Here we briefly review current knowledge regarding \TSPO\ and the implications of the new structures with respect to hypotheses and controversies in the field.

@article{Li2015TSPOCrystal, abstract = {Abstract The translocator protein 18 kDa (TSPO) has been the focus of intense research by the biomedical community and the pharmaceutical industry because of its apparent involvement in many disease-related processes. These include steroidogenesis, apoptosis, inflammation, neurological disease and cancer, resulting in the use of \{TSPO\} as a biomarker and its potential as a drug target. Despite more than 30 years of study, the precise function of \{TSPO\} remains elusive. A recent breakthrough in determining the high-resolution crystal structures of bacterial homologs of mitochondrial \{TSPO\} provides new insight into the structural and functional properties at a molecular level and new opportunities for investigating the significance of this ancient and highly conserved protein family. The availability of atomic level structural information from different species also provides a platform for structure-based drug development. Here we briefly review current knowledge regarding \{TSPO\} and the implications of the new structures with respect to hypotheses and controversies in the field. }, added-at = {2016-01-11T22:27:24.000+0100}, author = {Li, Fei and Liu, Jian and Garavito, R. Michael and Ferguson-Miller, Shelagh}, biburl = {https://www.bibsonomy.org/bibtex/20b1e89cd04933bcca946037a347f5a33/salotz}, description = {Evolving understanding of translocator protein 18kDa (TSPO)}, doi = {http://dx.doi.org/10.1016/j.phrs.2015.03.022}, interhash = {cfa7e295d8b8a1a0fde3befab8d291b0}, intrahash = {0b1e89cd04933bcca946037a347f5a33}, issn = {1043-6618}, journal = {Pharmacological Research }, keywords = {TSPO crystallography}, pages = {404 - 409}, timestamp = {2016-01-11T22:27:24.000+0100}, title = {Evolving understanding of translocator protein 18 kDa (TSPO) }, url = {http://www.sciencedirect.com/science/article/pii/S1043661815000626}, volume = 99, year = 2015 }