7vi0

Crystal structure of EP300 HAT domain in complex with compound 11

spinqualitylabelsall models 7vi0, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: 6YI, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed EP300 and its paralog CBP play an important role in post-translational modification as histone acetyltransferases (HATs). EP300/CBP inhibition has been gaining attention as an anticancer treatment target in recent years. Herein, we describe the identification of a novel, highly selective EP300/CBP inhibitor, compound 11 (DS17701585), by scaffold hopping and structure-based optimization of a high-throughput screening hit 1. Compound 11 (DS17701585) shows dose-dependent inhibition of SRY-box transcription factor 2 (SOX2) mRNA expression in a human lung squamous cell carcinoma cell line LK2-xenografted mouse model. Discovery of EP300/CBP histone acetyltransferase inhibitors through scaffold hopping of 1,4-oxazepane ring.,Kanada R, Kagoshima Y, Asano M, Suzuki T, Murata T, Haruta M, Takahashi M, Ubukata O, Hashimoto K, Obata K, Kihara K, Kuroha M, Banjo T, Togashi N, Sato K, Yamamoto Y, Suzuki K, Isoyama T, Tominaga Y, Higuchi S, Naito H Bioorg Med Chem Lett. 2022 Apr 9;66:128726. doi: 10.1016/j.bmcl.2022.128726. PMID:35413416 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone acetyltransferase 3D structures

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