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The structure of membrane associated proteins in eicosanoid and glutathione metabolism as determined by electron crystallography
KTH, School of Technology and Health (STH), Structural Biotechnology.ORCID iD: 0000-0002-3220-9402
2007 (English)In: Current opinion in structural biology, ISSN 0959-440X, E-ISSN 1879-033X, Vol. 17, no 4, 396-404 p.Article, review/survey (Refereed) Published
Abstract [en]

Membrane associated proteins in eicosanoid and glutathione metabolism (MAPEG) are involved in biosynthesis of arachidonic-derived mediators of pain, fever, and inflammation as well as in biotransformation and detoxification of electrophilic substances. Structure determination of microsomal glutathione transferase 1 using electron crystallography has provided the first atomic model of an MAPEG member. The homotrimer consists of three repeats of a four-helix transmembrane bundle with the largest extramembranous domain connecting the first and second helix and with a short proline rich loop on the same side between helices three and four. Residues of importance for intramolecular or intermolecular contacts as well as for stabilizing the active site have been identified and the results can be applied for interpreting structure-function relationship for similar MAPEG members.

Place, publisher, year, edition, pages
2007. Vol. 17, no 4, 396-404 p.
Keyword [en]
leukotriene c-4 synthase, prostaglandin-e synthase-1, site-directed mutagenesis, 6 angstrom resolution, projection structure, 2-dimensional crystallization, functional-characterization, crystal-structure, binding sites, s-transferase
URN: urn:nbn:se:kth:diva-17070DOI: 10.1016/ 000250423800003ScopusID: 2-s2.0-34548853132OAI: diva2:335113
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2010-10-04Bibliographically approved

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