Abstract:
:Ataxin-1 is a human protein responsible for spinocerebellar ataxia type 1, a hereditary disease associated with protein aggregation and misfolding. Essential for ataxin-1 aggregation is the anomalous expansion of a polyglutamine tract near the protein N-terminus, but the sequence-wise distant AXH domain modulates and contributes to the process. The AXH domain is also involved in the nonpathologic functions of the protein, including a variety of intermolecular interactions with other cellular partners. The domain forms a globular dimer in solution and displays a dimer of dimers arrangement in the crystal asymmetric unit. Here, we have characterized the domain further by studying its behavior in the crystal and in solution. We solved two new structures of the domain crystallized under different conditions that confirm an inherent plasticity of the AXH fold. In solution, the domain is present as a complex equilibrium mixture of monomeric, dimeric, and higher molecular weight species. This behavior, together with the tendency of the AXH fold to be trapped in local conformations, and the multiplicity of protomer interfaces, makes the AXH domain an unusual example of a chameleon protein whose properties bear potential relevance for the aggregation properties of ataxin-1 and thus for disease.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
de Chiara C,Rees M,Menon RP,Pauwels K,Lawrence C,Konarev PV,Svergun DI,Martin SR,Chen YW,Pastore Adoi
10.1016/j.bpj.2013.01.048subject
Has Abstractpub_date
2013-03-19 00:00:00pages
1304-13issue
6eissn
0006-3495issn
1542-0086pii
S0006-3495(13)00181-1journal_volume
104pub_type
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