The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The solution structure of the Josephin domain of ataxin-3: Structural determinants for molecular recognition
Open accessAbstract
The Josephin domain plays an important role in the cellular functions of ataxin-3, the protein responsible for the neurodegenerative Machado–Joseph disease. We have determined the solution structure of Josephin and shown that it belongs to the family of papain-like cysteine proteases, sharing the highest degree of structural similarity with bacterial staphopain. A currently unique structural feature of Josephin is a flexible helical hairpin formed by a 32-residue insertion, which could determine substrate specificity. By using the Josephin structure and the availability of NMR chemical shift assignments, we have mapped the enzyme active site by using the typical cysteine protease inhibitors, transepoxysuccinyl- l -eucylamido-4-guanidino-butane (E-64) and [ l -3-trans-(propylcarbamyl)oxirane-2-carbonyl]- l -isoleucyl- l -proline (CA-074). We also demonstrate that the specific interaction of Josephin with the ubiquitin-like domain of the ubiquitin- and proteasome-binding factor HHR23B involves complementary exposed hydrophobic surfaces. The structural similarity with other deubiquitinating enzymes suggests a model for the proteolytic enzymatic activity of ataxin-3.
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Cites
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical Information
Dominguez, C., Boelens, R., & Bonvin, A. M. J. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja026939x · Cited by 3,187
Toxic Proteins in Neurodegenerative Disease
Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251
Cited by
Breaking the chains: structure and function of the deubiquitinases
Komander, D., Clague, M. J., & Urbé, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2731 · Cited by 1,969
A genomic and functional inventory of deubiquitinating enzymes.
Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R. (2005) · Cell · doi:10.1016/j.cell.2005.11.007 · Cited by 1,854
Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.
Reyes-Turcu, F. E., Ventii, K. H., & Wilkinson, K. D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.082307.091526 · Cited by 1,396
Trinucleotide Repeat Disorders
Orr, H. T., & Zoghbi, H. Y. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.113042 · Cited by 1,368
The emerging complexity of protein ubiquitination
Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821
Metadata
- Authors
- Nicastro, G., Menon, R. P., Masino, L., Knowles, P. P., McDonald, N. Q., & Pastore, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-07-14
- Volume
- 102
- Issue
- 30
- Pages
- 10493-10498
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2004879226
- Cited by
- 188
- References
- 3
- FWCI
- 4.64
- Type
- journal article
- Language
- en
- Open access
- green
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- Nicastro, G., Menon, R. P., Masino, L., Knowles, P. P., McDonald, N. Q., & Pastore, A. (2005). The solution structure of the Josephin domain of ataxin-3: Structural determinants for molecular recognition. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0501732102
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