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 language | English |
|---|---|
| Article number | e107005 |
| Journal | PLoS One |
| Volume | 9 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 2014 Sep 5 |
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ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Medicine(all)
Cite this
Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site. / Jang, Tae Ho; Lee, Dong Sup; Choi, Kihang; Jeong, Eui Man; Kim, In Gyu; Kim, Young Whan; Chun, Jung Nyeo; Jeon, Ju Hong; Park, Hyun Ho.
In: PLoS One, Vol. 9, No. 9, e107005, 05.09.2014.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site
AU - Jang, Tae Ho
AU - Lee, Dong Sup
AU - Choi, Kihang
AU - Jeong, Eui Man
AU - Kim, In Gyu
AU - Kim, Young Whan
AU - Chun, Jung Nyeo
AU - Jeon, Ju Hong
AU - Park, Hyun Ho
PY - 2014/9/5
Y1 - 2014/9/5
N2 - 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
AB - 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
UR - http://www.scopus.com/inward/record.url?scp=84906996344&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84906996344&partnerID=8YFLogxK
U2 - 10.1371/journal.pone.0107005
DO - 10.1371/journal.pone.0107005
M3 - Article
C2 - 25192068
AN - SCOPUS:84906996344
VL - 9
JO - PLoS One
JF - PLoS One
SN - 1932-6203
IS - 9
M1 - e107005
ER -