3E4A

Human IDE-inhibitor complex at 2.6 angstrom resolution

3E4A の概要

• エントリーDOI: 10.2210/pdb3e4a/pdb
• 分子名称: Insulin-degrading enzyme, HYDROXAMATE PEPTIDE II1, ZINC ION, ... (7 entities in total)
• 機能のキーワード: insulin, hydroxamate, insulin degrading enzyme, hydrolase, metal-binding, metalloprotease, protease
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: P14735
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 239073.28

構造登録者

Malito, E.,Leissring, M.A.,Choi, S.,Cuny, G.D.,Tang, W.J. (登録日: 2008-08-11, 公開日: 2009-05-19, 最終更新日: 2023-08-30)

主引用文献

Leissring, M.A.,Malito, E.,Hedouin, S.,Reinstatler, L.,Sahara, T.,Abdul-Hay, S.O.,Choudhry, S.,Maharvi, G.M.,Fauq, A.H.,Huzarska, M.,May, P.S.,Choi, S.,Logan, T.P.,Turk, B.E.,Cantley, L.C.,Manolopoulou, M.,Tang, W.J.,Stein, R.L.,Cuny, G.D.,Selkoe, D.J.
Designed inhibitors of insulin-degrading enzyme regulate the catabolism and activity of insulin.
Plos One, 5:e10504-e10504, 2010

PubMed Abstract: Insulin is a vital peptide hormone that is a central regulator of glucose homeostasis, and impairments in insulin signaling cause diabetes mellitus. In principle, it should be possible to enhance the activity of insulin by inhibiting its catabolism, which is mediated primarily by insulin-degrading enzyme (IDE), a structurally and evolutionarily distinctive zinc-metalloprotease. Despite interest in pharmacological inhibition of IDE as an attractive anti-diabetic approach dating to the 1950s, potent and selective inhibitors of IDE have not yet emerged.

PubMed: 20498699
DOI: 10.1371/journal.pone.0010504

実験手法

X-RAY DIFFRACTION (2.6 Å)