1V06

AXH domain of the transcription factor HBP1 from M.musculus

1V06 の概要

• エントリーDOI: 10.2210/pdb1v06/pdb
• 分子名称: HMG BOX-CONTAINING PROTEIN 1 (1 entity in total)
• 機能のキーワード: 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
• 由来する生物種: MUS MUSCULUS (MOUSE)
• 細胞内の位置: Nucleus: Q8R316
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15775.75

構造登録者

De Chiara, C.,Kelly, G.,Pastore, A. (登録日: 2004-03-24, 公開日: 2005-04-21, 最終更新日: 2024-05-15)

主引用文献

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

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: 15893665
DOI: 10.1016/J.STR.2005.02.016

実験手法

SOLUTION NMR