4PYG

Transglutaminase2 complexed with GTP

4PYG の概要

• エントリーDOI: 10.2210/pdb4pyg/pdb
• 分子名称: Protein-glutamine gamma-glutamyltransferase 2, GUANOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: protein-gtp complex, transglutaminase fold, crosslinking, gtp binding, no modification, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 237021.10

構造登録者

Park, H.H.,Jang, T.H. (登録日: 2014-03-27, 公開日: 2015-02-11, 最終更新日: 2024-10-30)

主引用文献

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.
Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site.
Plos One, 9:e107005-e107005, 2014

PubMed 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.

PubMed: 25192068
DOI: 10.1371/journal.pone.0107005

実験手法

X-RAY DIFFRACTION (2.8 Å)