Structural aspects of transglutaminase 2: functional, structural, and regulatory diversity

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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