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Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis

Authors :
Madhuranayaki Thulasingam
Laura Orellana
Emmanuel Nji
Shabbir Ahmad
Agnes Rinaldo-Matthis
Jesper Z. Haeggström
Source :
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Publication Year :
2021
Publisher :
Nature Portfolio, 2021.

Abstract

Microsomal glutathione S-transferase 2 (MGST2) produces leukotriene C4, an intracrine mediator of cell death. Structural, biochemical and computational analyses of human MGST2 suggest a mechanism employed by the enzyme to restrict catalysis to only one active site within the MGST2 trimer.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
12
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.8bc33695d24df2a94e100658df694b
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-021-21924-8