The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
Open accessAbstract
The N-terminal domain of HIV-1 integrase contains a pair of His and Cys residues (the HHCC motif) that are conserved among retroviral integrases. Although His and Cys residues are often involved in binding zinc, the HHCC motif does not correspond to any recognized class of zinc binding domain. We have investigated the binding of zinc to HIV-1 integrase protein and find that it binds zinc with a stoichiometry of one zinc per integrase monomer. Analysis of zinc binding to deletion derivatives of integrase locates the binding site to the N-terminal domain. Integrase with a mutation in the HHCC motif does not bind zinc, consistent with coordination of zinc by these residues. The isolated N-terminal domain is disordered in the absence of zinc but, in the presence of zinc, it adopts a secondary structure with a high alpha helical content. Integrase bound by zinc tetramerizes more readily than the apoenzyme and is also more active than the apoenzyme in in vitro integration assays. We conclude that binding of zinc to the HHCC motif stabilizes the folded state of the N-terminal domain of integrase and bound zinc is required for optimal enzymatic activity.
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Dyda, F., Hickman, A. B., Jenkins, T. M., Engelman, A., Craigie, R., & Davies, D. R. (1994) · Science · doi:10.1126/science.7801124 · Cited by 810
Self-citationEngelman, A., & Craigie, R. (1992) · Journal of Virology · doi:10.1128/jvi.66.11.6361-6369.1992 · Cited by 519
Self-citationBrown, P. O., Bowerman, B., Varmus, H. E., & Bishop, J. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.8.2525 · Cited by 399
Retroviral DNA integration: structure of an integration intermediate
Fujiwara, T., & Mizuuchi, K. (1988) · Cell · doi:10.1016/0092-8674(88)90071-2 · Cited by 385
Solution Structure of the DNA Binding Domain of HIV-1 Integrase
Lodi, P. J., Ernst, J. A., Kuszewski, J., Hickman, A. B., Engelman, A., Craigie, R., Clore, G. M., & Gronenborn, A. M. (1995) · Biochemistry · doi:10.1021/bi00031a002 · Cited by 300
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Piana, S., Donchev, A. G., Robustelli, P., & Shaw, D. E. (2015) · The Journal of Physical Chemistry B · doi:10.1021/jp508971m · Cited by 852
Physicochemical Properties of Cells and Their Effects on Intrinsically Disordered Proteins (IDPs)
Theillet, F.-X., Binolfi, A., Frembgen-Kesner, T., Hingorani, K., Sarkar, M., Kyne, C., Li, C., Crowley, P. B., Gierasch, L., Pielak, G. J., et al. (2014) · Chemical Reviews · doi:10.1021/cr400695p · Cited by 503
Structural biology of HIV 1 1Edited by P. E. Wright
Turner, B. G., & Summers, M. F. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2354 · Cited by 470
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Metadata
- Authors
- Zheng, R., Jenkins, T. M., & Craigie, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-11-26
- Volume
- 93
- Issue
- 24
- Pages
- 13659-13664
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2032891258
- Cited by
- 341
- References
- 5
- FWCI
- 13.52
- Type
- journal article
- Language
- en
- Open access
- green
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- Zheng, R., Jenkins, T. M., & Craigie, R. (1996). Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.24.13659
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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