2jqd
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Revision as of 06:37, 24 April 2008
Structure of the Leucine-Rich Repeat domain of LANP
Overview
The leucine-rich repeat acidic nuclear protein (Anp32a/LANP) belongs to a family of evolutionarily-conserved phosphoproteins involved in a complex network of protein-protein interactions. In an effort to understand the cellular role, we have investigated the mode of interaction of Anp32a with its partners. As a prerequisite, we solved the structure in solution of the evolutionarily conserved N-terminal leucine-rich repeat (LRR) domain and modeled its interactions with other proteins, taking PP2A as a paradigmatic example. The interaction between the Anp32a LRR domain and the AXH domain of ataxin-1 was probed experimentally. The two isolated and unmodified domains bind with very weak (millimolar) affinity, thus suggesting the necessity either for an additional partner (e.g. other regions of either or both proteins or a third molecule) or for a post-translational modification. Finally, we identified by two-hybrid screening a new partner of the LRR domain, i.e. the microtubule plus-end tracking protein Clip 170/Restin, known to regulate the dynamic properties of microtubules and to be associated with severe human pathologies.
About this Structure
2JQD is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural bases for recognition of Anp32/LANP proteins., de Chiara C, Menon RP, Pastore A, FEBS J. 2008 Apr 10;. PMID:18410380 Page seeded by OCA on Thu Apr 24 09:37:15 2008
