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Updated: Feb 27, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Structural aspects of transglutaminase 2: functional, structural, and regulatory diversity
1College of Pharmacy and Research Institute of Pharmaceutical Science, Gyeongsang National University, Jinju, 52828, South Korea.
Abstract:
Transglutaminase 2 (TG2) is a multi-functional protein that has both protein cross-linking and guanosine 5'-triphosphate (GTP) hydrolysis activities. The activities of this protein are controlled by many cellular factors, including calcium (Ca2+) and GTP, and have been implicated in several physiological activities, including apoptosis, angiogenesis, wound healing, cellular differentiation, neuronal regeneration, and bone development. TG2 is linked to many human diseases such as inflammatory disease, celiac disease, neurodegenerative disease, diabetes, tissue fibrosis, and various cancers and is one of the most dynamic enzymes in terms of its functions, structures, and regulatory mechanisms. The aim of this review was to summarize the functional, structural, and regulatory diversity of TG2, with a particular focus on the structure of TG2.
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