3LY6

Crystal structure of human transglutaminase 2 complex with adenosine 5' Triphosphate

3LY6 の概要

• エントリーDOI: 10.2210/pdb3ly6/pdb
• 分子名称: Protein-glutamine gamma-glutamyltransferase 2, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: transglutaminase, acyltransferase, diabetes mellitus, disease mutation, metal-binding, phosphoprotein, 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: 237675.73

構造登録者

Han, B.G.,Lee, B.I. (登録日: 2010-02-26, 公開日: 2010-08-18, 最終更新日: 2024-11-20)

主引用文献

Han, B.G.,Cho, J.W.,Cho, Y.D.,Jeong, K.C.,Kim, S.Y.,Lee, B.I.
Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate
Int.J.Biol.Macromol., 47:190-195, 2010

PubMed Abstract: Transglutaminase 2 (TG2) is a calcium-dependent multifunctional protein associated with various human diseases. We determined the crystal structure of human TG2 in complex with adenosine triphosphate (ATP). The ATP molecule binds to the previously identified guanosine diphosphate (GDP) binding pocket but has different hydrogen bonds and ion interaction with protein. The four residues Arg476, Arg478, Val479 and Tyr583, all of which are involved in both ATP and GDP binding by hydrogen bonds, might play important roles in the stabilization of TG2 by ATP or GDP. However, Ser482 and Arg580, which are involved in GDP binding, do not form hydrogen bond with ATP. Additionally, we newly discovered an intramolecular disulfide bond between Cys230 and Cys370, which formation might regulate the enzymatic activity of TG2.

PubMed: 20450932
DOI: 10.1016/j.ijbiomac.2010.04.023

実験手法

X-RAY DIFFRACTION (3.14 Å)