Structure validation of the Josephin domain of ataxin-3: Conclusive evidence 
for an open conformation

Nicastro, G; Habeck, M; Masino, L; Svergun, DI; Pastore, A

doi:10.1007/s10858-006-9092-z

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Structure validation of the Josephin domain of ataxin-3: Conclusive evidence for an open conformation

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Habeck, M
Department Empirical Inference, Max Planck Institute for Biological Cybernetics, Max Planck Society;

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https://link.springer.com/content/pdf/10.1007%2Fs10858-006-9092-z.pdf
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Citation

Nicastro, G., Habeck, M., Masino, L., Svergun, D., & Pastore, A. (2006). Structure validation of the Josephin domain of ataxin-3: Conclusive evidence for an open conformation. Journal of Biomolecular NMR, 36(4), 267-277. doi:10.1007/s10858-006-9092-z.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0013-CF43-8

Abstract

The availability of new and fast tools in structure determination has led to a more than exponential growth of the number of structures solved per year. It is therefore increasingly essential to assess the accuracy of the new structures by reliable approaches able to assist validation. Here, we discuss a specific example in which the use of different complementary techniques, which include Bayesian methods and small angle scattering, resulted essential for validating the two currently available structures of the Josephin domain of ataxin-3, a protein involved in the ubiquitin/proteasome pathway and responsible for neurodegenerative spinocerebellar ataxia of type 3. Taken together, our results demonstrate that only one of the two structures is compatible with the experimental information. Based on the high precision of our refined structure, we show that Josephin contains an open cleft which could be directly implicated in the interaction with polyubiquitin chains and other partners.