Synovial sarcoma (SS) is a rare malignancy that accounts for 8% to 10% of all soft-tissue malignancies. In all cases the pathogenic fusion protein SS18-SSX is produced by a recurrent chromosomal translocation, t(X;18)(p11.2;q11.2), suggesting that when it binds to the ATP-dependent mammalian chromatin remodeling complex SWI/SNF (mSWI/SNF) it forms an aberrant complex. This abnormal mSWI/SNF complex causes deviation from the normal pattern of gene expression, leading to the belief that it is the trigger for SS. The incorporation of SSX region, especially those that are not originally components of the mSWI/SNF complex, is considered to be the first step. Noting that SSX has been reported to bind to nucleosomes using its C-terminal 34 residues (SSXRD), we conducted experiments to elucidate the mode of interaction between SSXRD and nucleosomes and to link the results to drug discovery. Although SSXRD is an intrinsically disordered region and structure-based drug design　
is a difficult target, its properties have been clarified from its structure through cryo-EM single particle analysis, NMR, HS-AFM and biochemical experiments. These advances have enabled the structural understanding of the interaction between SSXRD and nucleosomes to open new opportunities for drug discovery.