Transcription factors, which bind DNA, and post-transcriptional regulators, which bind RNA, together form a complex system that coordinates the level to which individual genes are expressed. In addition, some proteins integrate the information from each regulatory network by interacting with both DNA and RNA. The classical zinc finger is a well-characterised DNA-binding domain that has been identified in more than 800 human proteins. However, some proteins utilise this domain to bind RNA, and little is known about how a single protein fold can achieve this dual functionality. In this project, the RNA-binding activity of the human ZNF180 protein was investigated. The iterative selection procedure SELEX was employed to determine the target binding sequence of a ZNF180 zinc finger construct. By deep sequencing the enriched library, RNA sequences and secondary structures bound by the zinc finger domains were identified. This improved understanding of the molecular mechanism by which zinc fingers recognise RNA will broaden our appreciation of the post-transcriptional activity of a large protein family that is currently assumed to be predominantly comprised of transcription factors.