REVIEWS  7th INTERNATIONAL CONFERENCE ON TRANSGLUTAMINASES AND PROTEIN CROSSLINKING REACTIONS
Ferrara (Italy), September 14-17, 2002 

Minerva Biotecnologica 2002 June;14(2):113-9

Copyright © 2003 EDIZIONI MINERVA MEDICA

lingua: Inglese

Structure and function of tissue transglutaminase

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.