5CI7

Structure of ULK1 bound to a selective inhibitor

5CI7 の概要

• エントリーDOI: 10.2210/pdb5ci7/pdb
• 関連するPDBエントリー: 4WNO
• 分子名称: Serine/threonine-protein kinase ULK1, N-[3-({4-[(3-aminopropyl)amino]-5-iodopyrimidin-2-yl}amino)phenyl]pyrrolidine-1-carboxamide, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: inhibitor, kinase, autophagy, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33077.88

構造登録者

Lazarus, M.B.,Shokat, K.M. (登録日: 2015-07-11, 公開日: 2015-08-26, 最終更新日: 2024-11-20)

主引用文献

Lazarus, M.B.,Shokat, K.M.
Discovery and structure of a new inhibitor scaffold of the autophagy initiating kinase ULK1.
Bioorg.Med.Chem., 23:5483-5488, 2015

PubMed Abstract: Energy homeostasis in eukaryotic cells is a complex and fundamental process that is misregulated in several human diseases. A key component of energy regulation is a process called autophagy that involves the recycling of cellular components. There has been much recent interest in studying the mechanism of autophagy to understand an important cellular process and to evaluate the therapeutic potential in targeting autophagy. Activation of a kinase called ULK1 initiates autophagy by driving downstream pathways that lead to the formation of double membrane bound vesicles that surround the cellular contents that are to be degraded. Here, we report the discovery of an inhibitor of ULK1 with improved selectivity and a high-resolution crystal structure of the compound bound to the kinase, which will be useful tools for studying autophagy in cells.

PubMed: 26275681
DOI: 10.1016/j.bmc.2015.07.034

実験手法

X-RAY DIFFRACTION (1.74 Å)