In this paper we examine this localized induced folding event in the context of the entire N TAIL domain. A low-resolution structural model of the complex between XD and N TAIL shows the presence of a bulky globular region and of an extended and elongated shape. The model shows that the N-terminal region of N TAIL (residues 401-488) remains predominantly unfolded, and the 489-525 region is packed against XD, thus suggesting that beyond the a-MoRE the C terminus may play a role in the interaction with XD. Indeed, we present several lines of experimental evidence confirming that beyond the region encompassing the a-MoRE, an additional N TAIL region encompassing residues 517-525 also contributes to binding to XD, although without undergoing any gain of regular secondary structure.