Crystal Structure of Transglutaminase 2 with GTP Complex and Amino Acid Sequence Evidence of Evolution of GTP Binding Site

Title
Crystal Structure of Transglutaminase 2 with GTP Complex and Amino Acid Sequence Evidence of Evolution of GTP Binding Site
Author(s)
박현호장태호이동섭[이동섭]최기항[최기항]정의만[정의만]김인규[김인규]김영환[김영환]천정녀[천정녀]전주홍[전주홍]
Keywords
TISSUE TRANSGLUTAMINASE; CROSS-LINKING; TUMOR-GROWTH; ALZHEIMERS-DISEASE; PROTEIN COMPLEXES; TGASE 3; IDENTIFICATION; CELLS; RAT; APOPTOSIS
Issue Date
201411
Publisher
PUBLIC LIBRARY SCIENCE
Citation
PLOS ONE, v.9, no.9
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.
URI
http://hdl.handle.net/YU.REPOSITORY/30483http://dx.doi.org/10.1371/journal.pone.0107005
ISSN
1932-6203
Appears in Collections:
이과대학 > 화학생화학부 > Articles
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