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Fig. 1 | Clinical Epigenetics

Fig. 1

From: Targeted design and identification of AC1NOD4Q to block activity of HOTAIR by abrogating the scaffold interaction with EZH2

Fig. 1

Schematic illustration of studying the structure and function of HOTAIR and identifying AC1NOD4Q as a small molecule inhibiting the HOTAIR/PRC2 complex interaction. The 5′ domain, but not the 3′ domain, proved to be the functional domain responsible for tumorigenesis in glioma and breast cancer. Further analysis demonstrated that the minimal HOTAIR domain required for PRC2 binding is 212–300 nt. Using 3D modeling prediction, we found that this domain contains several hairpin loop structures and serves as a target for small molecule intervention. By performing in silico high-throughput screening, we determined that AC1NOD4Q binds at a specific HOTAIR micro-domain (36G46A) and induces strong molecular inference in the scaffold interaction between the PRC2 complex and HOTAIR

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