Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity.

@article{Begg2006MutationOA,
  title={Mutation of a critical arginine in the GTP-binding site of transglutaminase 2 disinhibits intracellular cross-linking activity.},
  author={Gillian E Begg and Sara R. Holman and Philippa H. Stokes and Jacqueline Mary Matthews and Robert M. Graham and Siiri E. Iismaa},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 18},
  pages={12603-9}
}
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. A., and Clardy, J. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 2743-2747), we have… CONTINUE READING

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