The AXH module: an independently folded domain common to ataxin‐1 and HBP1

FEBS Letters

Pastore, A.²  Adinolfi, S.²  de Boer, J.²  Ramos, A.²  Guida, S.¹  Jodice, C.¹  de Chiara, C.²  Giannini, C.²  Kioussis, D.² 

[1] Dipartimento di Biologia, Università di Tor Vergata, via della Ricerca Scientifica, 00133 Rome, Italy;National Institute for Medical Research, The Ridgeway, London NW71AA, UK

关键词: Misfolding disease;    Poly-glutamine;    Protein module;    SCA1;    Structure;   

DOI  :  10.1016/S0014-5793(03)00818-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Ataxin-1 (ATX1), a human protein responsible for spinocerebellar ataxia type 1 in humans, shares a region of homology, named AXH module, with the apparently unrelated transcription factor HBP1. Here, we describe the first characterisation of the AXH module in terms of its structural properties and stability. By producing protein constructs spanning the AXH modules of ATX1 and HBP1 and by comparing their properties, we have identified the minimal region sufficient for forming independently folded units (domains). Knowledge of the AXH domain boundaries allows us to map many of the interactions of ATX1 with other molecules onto the AXH module. We further show that the AXH of ATX1 is a dimerisation domain and is able to recognise RNA with the same nucleotide preference previously described for the full-length protein. AXH is therefore a novel protein–protein and RNA binding motif.

【 授权许可】

Unknown