1V06
AXH domain of the transcription factor HBP1 from M.musculus
Summary for 1V06
| Entry DOI | 10.2210/pdb1v06/pdb |
| Descriptor | HMG BOX-CONTAINING PROTEIN 1 (1 entity in total) |
| Functional Keywords | dna-binding protein, transcription factor, protein-protein interaction, nucleic acid binding, ob-fold, ataxin-1 homologous, repressor, transcription, transcription regulation, wnt signaling pathway, dna binding protein |
| Biological source | MUS MUSCULUS (MOUSE) |
| Cellular location | Nucleus: Q8R316 |
| Total number of polymer chains | 1 |
| Total formula weight | 15775.75 |
| Authors | De Chiara, C.,Kelly, G.,Pastore, A. (deposition date: 2004-03-24, release date: 2005-04-21, Last modification date: 2024-05-15) |
| Primary citation | De Chiara, C.,Menon, R.P.,Adinolfi, S.,De Boer, J.,Ktistaki, E.,Kelly, G.,Calder, L.,Kioussis, D.,Pastore, A. The Axh Domain Adopts Alternative Folds the Solution Structure of Hbp1 Axh. Structure, 13:743-, 2005 Cited by PubMed Abstract: AXH is a protein module identified in two unrelated families that comprise the transcriptional repressor HBP1 and ataxin-1 (ATX1), the protein responsible for spinocerebellar ataxia type-1 (SCA1). SCA1 is a neurodegenerative disorder associated with protein misfolding and formation of toxic intranuclear aggregates. We have solved the structure in solution of monomeric AXH from HBP1. The domain adopts a nonclassical permutation of an OB fold and binds nucleic acids, a function previously unidentified for this region of HBP1. Comparison of HBP1 AXH with the crystal structure of dimeric ATX1 AXH indicates that, despite the significant sequence homology, the two proteins have different topologies, suggesting that AXH has chameleon properties. We further demonstrate that HBP1 AXH remains monomeric, whereas the ATX1 dimer spontaneously aggregates and forms fibers. Our results describe an entirely novel, to our knowledge, example of a chameleon fold and suggest a link between these properties and the SCA1 pathogenesis. PubMed: 15893665DOI: 10.1016/J.STR.2005.02.016 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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