Chromatin is constantly remodelled through the exchange, movement and replacement of histone subunits. This remodelling is an essential step in all aspects of genome biology ranging from transcription to DNA replication and repair. The remodelling process is orchestrated by large multi-protein complexes that must be recruited to appropriate target sites to carry out their function. The question of how remodelling complexes are recruited to target sites is, at the moment, largely unanswered at the molecular level. We have focused recently on understanding the structure and function of the Nucleosome Remodelling and Deacetylase (NuRD) complex, a complex of at least 10 proteins that is essential for development, stem cell renewal and differentiation. As part of this initiative, we have used solution NMR spectroscopy and other complementary methods to investigate interactions between NuRD protein components and gene-specific regulatory proteins. Data from this structural work allows us to draw broad conclusions about how NuRD and other remodelling complexes find their cognate target sites in several billion base pairs of DNA.