Abstract
The Leucine-rich repeat Acidic Nuclear Protein (LANP/Anp32a) is a member of the Anp32 family of acidic nuclear phosphoproteins, which is characterized by the presence of an amino terminal domain containing leucine-rich repeats (LRR) and of a carboxylterminal low complexity acidic region (Chen et al. 1996: Matilla and Radrizzani 2005). Members of the family have been associated with different activities, i.e., tumour suppression, RNA shuttling, transcriptional regulation, modulation of apoptosis and cerebellar morphogenesis. The LRR N-terminus of LANP/ Anp32a is a structural domain that is crucial for protein-protein interactions and accounts for the interaction with several partners including the nuclear export receptor CRM1, and the neurodegenerative disease-related protein ataxin-1. As the first step to the structure determination of LANP/Anp32a we report the virtually complete assignment of the backbone and side-chain H, C and N nuclei of the LRR domain (1-164). The data are deposited in BMRB with accession number 7081.
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