The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A
Open accessAbstract
Packaging of cyclophilin A (CypA) into HIV-1 virions is essential for efficient replication; however, the reason for this is unknown. Incorporation is mediated through binding to the Gly-89–Pro-90 peptide bond of the N-terminal domain of HIV-1 capsid (CA N ). Despite the fact that CypA is a peptidyl-prolyl cis/trans isomerase, catalytic activity on CA N has not been observed previously. We show here, using NMR exchange spectroscopy, that CypA does not only bind to CA N but also catalyzes efficiently the cis/trans isomerization of the Gly-89–Pro-90 peptide bond. In addition, conformational changes in CA N distal to the CypA binding loop are observed on CypA binding and catalysis. The results provide experimental evidence for efficient CypA catalysis on a natively folded and biologically relevant protein substrate.
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Cites
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
The mechanism of action of cyclosporin A and FK506
Schreiber, S. L., & Crabtree, G. R. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90111-j · Cited by 2,127
Specific incorporation of cyclophilin A into HIV-1 virions
Franke, E. K., Yuan, H. E. H., & Luban, J. (1994) · Nature · doi:10.1038/372359a0 · Cited by 745
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein
Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721
Crystal Structure of Human Cyclophilin A Bound to the Amino-Terminal Domain of HIV-1 Capsid
Gamble, T. R., Vajdos, F. F., Yoo, S., Worthylake, D. K., Houseweart, M., Sundquist, W. I., & Hill, C. P. (1996) · Cell · doi:10.1016/s0092-8674(00)81823-1 · Cited by 706
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Cited by
Allosteric regulation and catalysis emerge via a common route
Goodey, N. M., & Benkovic, S. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.98 · Cited by 667
The structural biology of HIV assembly
Ganser-Pornillos, B. K., Yeager, M., & Sundquist, W. I. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.02.001 · Cited by 503
Self-citationAn NMR Perspective on Enzyme Dynamics
Boehr, D. D., Dyson, H. J., & Wright, P. E. (2006) · Chemical Reviews · doi:10.1021/cr050312q · Cited by 458
HIV-1 capsid: the multifaceted key player in HIV-1 infection
Campbell, E. M., & Hope, T. J. (2015) · Nature Reviews Microbiology · doi:10.1038/nrmicro3503 · Cited by 430
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
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Metadata
- Authors
- Bosco, D. A., Eisenmesser, E. Z., Pochapsky, S., Sundquist, W. I., & Kern, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-04-02
- Volume
- 99
- Issue
- 8
- Pages
- 5247-5252
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1975534778
- Cited by
- 229
- References
- 5
- FWCI
- 4.32
- Type
- journal article
- Language
- en
- Open access
- green
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- Bosco, D. A., Eisenmesser, E. Z., Pochapsky, S., Sundquist, W. I., & Kern, D. (2002). Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.082100499
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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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