Zinc finger (ZF) proteins make up a large family of metalloproteins that contain discrete domains with amino acid ligands (cysteine and histidine) that serve to coordinate zinc in a tetrahedral geometry. Upon zinc coordination, the domains adopt three-dimensional structure. The most well-studied ZFs are the "classical" ZFs, which use a Cys2His2 motif to bind zinc and adopt an antiparallel β sheet/α helical fold. In addition to the classical ZF class, at least 13 other ZF classes, collectively termed nonclassical ZFs, have been identified. These other classes are distinguished by the combination and order of the cysteine and histidine ligands within each domain, the spacing between each ligand (i.e., number and type of amino acid), and the structural architecture that the domain adopts in the presence of zinc. One class of nonclassical ZFs, the neural zinc finger/myelin transcription factor (NZF/MyT) class, contains ZF domains with a Cys2His2Cys ligand set, adopts a fold that consists of a series of loops in the presence of zinc, and functions as transcription factors by binding to and regulating genes that are critical for the development of the central nervous system. This Current Topic focuses on our understanding of the NZF/MyT class of nonclassical ZFs and presents current hypotheses regarding this class' unique mechanism of metal-mediated folding and function.