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

doi:10.1371/journal.pone.0107005

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

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

27 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 language	English
Article number	e107005
Journal	PloS one
Volume	9
Issue number	9
DOIs	https://doi.org/10.1371/journal.pone.0107005
Publication status	Published - 2014 Sep 5

ASJC Scopus subject areas

General

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1371/journal.pone.0107005

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 › peer-review

@article{c7ae5863dfca4aa6a415d00cda6f9361,

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

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",

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

note = "Publisher Copyright: {\textcopyright} 2014 Jang et al.",

year = "2014",

month = sep,

day = "5",

doi = "10.1371/journal.pone.0107005",

language = "English",

volume = "9",

journal = "PLoS One",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "9",

}

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

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 -

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

Abstract

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this