Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation.

@article{Ahvazi2002ThreedimensionalSO,
  title={Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation.},
  author={Bijan Ahvazi and Hee Chul Kim and Sun-Ho Kee and Zolt{\'a}n Nemes and Peter M. Steinert},
  journal={The EMBO journal},
  year={2002},
  volume={21 9},
  pages={2055-67}
}
Transglutaminase (TGase) enzymes catalyze the formation of covalent cross-links between protein-bound glutamines and lysines in a calcium-dependent manner, but the role of Ca(2+) ions remains unclear. The TGase 3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. We have solved the three-dimensional structures of the zymogen and the activated forms at 2.2 and 2.1 A resolution, respectively, and examined the role of… CONTINUE READING

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