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Indexed/Abstracted in: EMBASE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 0,246
Online ISSN 1827-160X
7th INTERNATIONAL CONFERENCE ON TRANSGLUTAMINASES AND PROTEIN CROSSLINKING REACTIONS
Ferrara (Italy), September 14-17, 2002
Iismaa S. E.
Victor Chang Cardiac Research Institute, Sydney, NSW, Australia
A detailed report on the structure and function of tissue transglutaminase is presented. The two distinct activities of TG2, which is a multifunctional protein, are examined: Ca2+-activated transamidation activity that is inhibited by GTP binding and receptor signalling activity that requires GTP binding. The recently solved crystal structure of GDP-bound TG2 indicates a novel fold for the GDP-binding site. In addition, evidence suggests TG2 also plays a major extracellular role in protein-protein interactions that are independent of its cross-linking activity.