The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
Open accessAbstract
Synthetic C peptides, corresponding to the C helix of the HIV type 1 (HIV-1) gp41 envelope protein, are potent inhibitors of HIV-1 membrane fusion. One such peptide is in clinical trials. The crystal structure of the gp41 core, in its proposed fusion-active conformation, is a trimer of helical hairpins in which three C helices pack against a central coiled coil. Each C helix shows especially prominent contacts with one of three symmetry-related, hydrophobic cavities on the surface of the coiled coil. We show that the inhibitory activity of the C peptide C34 depends on its ability to bind to this coiled-coil cavity. Moreover, examining a series of C34 peptide variants with modified cavity-binding residues, we find a linear relationship between the logarithm of the inhibitory potency and the stability of the corresponding helical-hairpin complexes. Our results provide strong evidence that this coiled-coil cavity is a good drug target and clarify the mechanism of C peptide inhibition. They also suggest simple, quantitative assays for the identification and evaluation of analogous inhibitors of HIV-1 entry.
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Self-citationAtomic structure of the ectodomain from HIV-1 gp41
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Cited by
Protein Design of an HIV-1 Entry Inhibitor
Root, M. J., Kay, M. S., & Kim, P. S. (2001) · Science · doi:10.1126/science.1057453 · Cited by 391
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Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
Bird, G. H., Madani, N., Perry, A. F., Princiotto, A. M., Supko, J. G., He, X., Gavathiotis, E., Sodroski, J. G., & Walensky, L. D. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002713107 · Cited by 347
Discovery and Optimization of a Natural HIV-1 Entry Inhibitor Targeting the gp41 Fusion Peptide
Münch, J., Ständker, L., Adermann, K., Schulz, A., Schindler, M., Chinnadurai, R., Pöhlmann, S., Chaipan, C., Biet, T., Peters, T., et al. (2007) · Cell · doi:10.1016/j.cell.2007.02.042 · Cited by 261
Cell surface receptors, virus entry and tropism of primate lentiviruses
Clapham, P. R., & McKnight, Á. (2002) · Journal of General Virology · doi:10.1099/0022-1317-83-8-1809 · Cited by 256
Metadata
- Authors
- Chan, D. C., Chutkowski, C. T., & Kim, P. S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-12-22
- Volume
- 95
- Issue
- 26
- Pages
- 15613-15617
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2030648131
- Cited by
- 477
- References
- 42
- FWCI
- 4.02
- Type
- journal article
- Language
- en
- Open access
- green
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- Chan, D. C., Chutkowski, C. T., & Kim, P. S. (1998). Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.26.15613
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
