Open AccessStructure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity
Author(s) -
Hyekyung Ha,
Sunghoon Kwon,
Eui Man Jeong,
Chang Min Kim,
Ki Baek Lee,
In Gyu Kim,
Hyun Ho Park
Publication year - 2018
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0204707
Subject(s) - tissue transglutaminase , biology , angiogenesis , wound healing , microbiology and biotechnology , apoptosis , biochemistry , enzyme , cancer research , immunology
Multi-functional transglutaminase 2 (TG2), which possesses protein cross-linking and GTP hydrolysis activities, is involved in various cellular processes, including apoptosis, angiogenesis, wound healing, and neuronal regeneration, and is associated with many human diseases, including inflammatory disease, celiac disease, neurodegenerative disease, diabetes, tissue fibrosis, and cancers. Although most biochemical and cellular studies have been conducted with the TG2 (G224) form, the TG2 (G224V) form has recently emerged as a putative natural variant of TG2. In this study, we characterized the putative natural form of TG2, TG2 (G224V), and through a new crystal structure of TG2 (G224V), we revealed how TG2 (G224V) gained stability and higher Ca 2+ -dependent activity than an artificial variant of TG2 (G224).