4FCK

Crystal Structure of the Co2+2-Human Arginase I-AGPA Complex

4FCK の概要

• エントリーDOI: 10.2210/pdb4fck/pdb
• 関連するPDBエントリー: 2PHA 4FCI
• 分子名称: Arginase-1, 2-AMINO-3-GUANIDINO-PROPIONIC ACID, COBALT (II) ION, ... (4 entities in total)
• 機能のキーワード: arginase fold, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70087.79

構造登録者

D'Antonio, E.L.,Christianson, D.W. (登録日: 2012-05-25, 公開日: 2012-06-20, 最終更新日: 2023-09-13)

主引用文献

D'Antonio, E.L.,Christianson, D.W.
Binding of the unreactive substrate analog L-2-amino-3-guanidinopropionic acid (dinor-L-arginine) to human arginase I.
Acta Crystallogr.,Sect.F, 68:889-893, 2012

PubMed Abstract: Human arginase I (HAI) is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of L-arginine to form L-ornithine and urea through a metal-activated hydroxide mechanism. Since HAI regulates L-Arg bioavailability for NO biosynthesis, it is a potential drug target for the treatment of cardiovascular diseases such as atherosclerosis. X-ray crystal structures are now reported of the complexes of Mn(2)(2+)-HAI and Co(2)(2+)-HAI with L-2-amino-3-guanidinopropionic acid (AGPA; also known as dinor-L-arginine), an amino acid bearing a guanidinium side chain two methylene groups shorter than that of L-arginine. Hydrogen bonds to the α-carboxylate and α-amino groups of AGPA dominate enzyme-inhibitor recognition; the guanidinium group does not interact directly with the metal ions.

PubMed: 22869115
DOI: 10.1107/S1744309112027820

実験手法

X-RAY DIFFRACTION (1.9 Å)