Article
Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity.
The Journal of biological chemistry - 5 May 2006
Begg Gillian E, Holman Sara R, Stokes Philippa H, Matthews Jacqueline M, Graham Robert M, Iismaa Siiri E
Abstract excerpt
Transglutaminase type 2 (TG2; also known as G(h)) is a multifunctional protein involved in diverse cellular processes. It has two well characterized enzyme activities: receptor-stimulated signaling that requires GTP binding and calcium-activated transamidation or cross-linking that is inhibited by GTP. In addition to the GDP binding residues identified from the human TG2 crystal structure (Liu, S., Cerione, R....
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