Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site

Tae Ho Jang, Dong Sup Lee, Kihang Choi, Eui Man Jeong, In Gyu Kim, Young Whan Kim, Jung Nyeo Chun, Ju Hong Jeon, Hyun Ho Park

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Transglutaminase2 (TG2) is a multi-functional protein involved in various cellular processes, including apoptosis, differentiation, wound healing, and angiogenesis. The malfunction of TG2 causes many human disease including inflammatory disease, celiac disease, neurodegenerative diseases, tissue fibrosis, and cancers. Protein cross-linking activity, which is representative of TG2, is activated by calcium ions and suppressed by GTP. Here, we elucidated the structure of TG2 in complex with its endogenous inhibitor, GTP. Our structure showed why GTP is the optimal nucleotide for interacting with and inhibiting TG2. In addition, sequence comparison provided information describing the evolutionary scenario of GTP usage for controlling the activity of TG2. Copyright

Original languageEnglish
Article numbere107005
JournalPLoS One
Volume9
Issue number9
DOIs
Publication statusPublished - 2014 Sep 5

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

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    Jang, T. H., Lee, D. S., Choi, K., Jeong, E. M., Kim, I. G., Kim, Y. W., Chun, J. N., Jeon, J. H., & Park, H. H. (2014). Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site. PLoS One, 9(9), [e107005]. https://doi.org/10.1371/journal.pone.0107005