2JQD
Structure of the Leucine-Rich Repeat domain of LANP
Summary for 2JQD
| Entry DOI | 10.2210/pdb2jqd/pdb |
| Descriptor | Acidic leucine-rich nuclear phosphoprotein 32 family member A (1 entity in total) |
| Functional Keywords | lanp/anp32a, lrr domain, phosphoprotein, pp2a inhibitor, tumor suppression, transcriptional regulation, rna shuttling, apoptosis, cerebellar morphogenesis, gene regulation, protein binding |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: O35381 |
| Total number of polymer chains | 1 |
| Total formula weight | 19213.93 |
| Authors | de Chiara, C.,Pastore, A. (deposition date: 2007-05-31, release date: 2008-04-22, Last modification date: 2024-05-29) |
| Primary citation | de Chiara, C.,Menon, R.P.,Pastore, A. Structural bases for recognition of Anp32/LANP proteins Febs J., 275:2548-2560, 2008 Cited by PubMed Abstract: 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. PubMed: 18410380DOI: 10.1111/j.1742-4658.2008.06403.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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