5K4L

Crystal structure of KDM5A in complex with a naphthyridone inhibitor

5K4L の概要

• エントリーDOI: 10.2210/pdb5k4l/pdb
• 分子名称: Lysine-specific demethylase 5A, Unknown Peptide, NICKEL (II) ION, ... (6 entities in total)
• 機能のキーワード: epigenetics, demethylase, jumonji, inhibitor, cancer, oxidoreductase-inhibitor complex, oxidoreductase/inhibitor
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus, nucleolus : P29375
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 183991.47

構造登録者

Kiefer, J.R.,Vinogradova, M.V. (登録日: 2016-05-20, 公開日: 2016-08-10, 最終更新日: 2024-10-23)

主引用文献

Labadie, S.S.,Dragovich, P.S.,Cummings, R.T.,Deshmukh, G.,Gustafson, A.,Han, N.,Harmange, J.C.,Kiefer, J.R.,Li, Y.,Liang, J.,Liederer, B.M.,Liu, Y.,Manieri, W.,Mao, W.,Murray, L.,Ortwine, D.F.,Trojer, P.,VanderPorten, E.,Vinogradova, M.,Wen, L.
Design and evaluation of 1,7-naphthyridones as novel KDM5 inhibitors.
Bioorg.Med.Chem.Lett., 26:4492-4496, 2016

PubMed Abstract: Features from a high throughput screening (HTS) hit and a previously reported scaffold were combined to generate 1,7-naphthyridones as novel KDM5 enzyme inhibitors with nanomolar potencies. These molecules exhibited high selectivity over the related KDM4C and KDM2B isoforms. An X-ray co-crystal structure of a representative molecule bound to KDM5A showed that these inhibitors are competitive with the co-substrate (2-oxoglutarate or 2-OG).

PubMed: 27499454
DOI: 10.1016/j.bmcl.2016.07.070

実験手法

X-RAY DIFFRACTION (3.179 Å)