6A8P

Transglutaminase 2 mutant G224V in complex with GTP

6A8P の概要

• エントリーDOI: 10.2210/pdb6a8p/pdb
• 分子名称: Protein-glutamine gamma-glutamyltransferase 2, GUANOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: transglutaminase, complex, mutant, gtp, 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.,Ha, H.J.,Kwon, S. (登録日: 2018-07-09, 公開日: 2018-09-26, 最終更新日: 2023-11-22)

主引用文献

Ha, H.J.,Kwon, S.,Jeong, E.M.,Kim, C.M.,Lee, K.B.,Kim, I.G.,Park, H.H.
Structure of natural variant transglutaminase 2 reveals molecular basis of gaining stability and higher activity.
PLoS ONE, 13:e0204707-e0204707, 2018

PubMed Abstract: Multi-functional transglutaminase 2 (TG2), which possesses protein cross-linking and GTP hydrolysis activities, is involved in various cellular processes, including apoptosis, angiogenesis, wound healing, and neuronal regeneration, and is associated with many human diseases, including inflammatory disease, celiac disease, neurodegenerative disease, diabetes, tissue fibrosis, and cancers. Although most biochemical and cellular studies have been conducted with the TG2 (G224) form, the TG2 (G224V) form has recently emerged as a putative natural variant of TG2. In this study, we characterized the putative natural form of TG2, TG2 (G224V), and through a new crystal structure of TG2 (G224V), we revealed how TG2 (G224V) gained stability and higher Ca2+-dependent activity than an artificial variant of TG2 (G224).

PubMed: 30321187
DOI: 10.1371/journal.pone.0204707

実験手法

X-RAY DIFFRACTION (2.537 Å)