The STIL protein contains intrinsically disordered regions that mediate its protein-protein interactionsElectronic supplementary information (ESI) available: Experimental details, a table and 2 figures. See DOI: 10.1039/c3cc45096a

The STIL protein participates in mitosis and malignant transformation by regulating centrosomal duplication. Using biophysical methods we studied the structure and interactions of STIL. We revealed that its central domain is intrinsically disordered and mediates protein-protein interactions of STIL. The intrinsic disorder may provide STIL with the conformational flexibility required for its multitude binding. Protein interactions of STIL are mediated through its intrinsically disordered domain, making this domain a new target for anti cancer drugs.