The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Structural Analysis of the Mechanism of Adenovirus Binding to Its Human Cellular Receptor, CAR
Abstract
Binding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high-affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors.
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Metadata
- Authors
- Bewley, M. C., Springer, K., Zhang, Y.-B., Freimuth, P., & Flanagan, J. M.
- Venue
- Science
- Published
- 1999-11-19
- Volume
- 286
- Issue
- 5444
- Pages
- 1579-1583
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2101305223
- Cited by
- 448
- References
- 20
- FWCI
- 18.07
- Type
- journal article
- Language
- en
- Open access
- closed
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- Bewley, M. C., Springer, K., Zhang, Y.-B., Freimuth, P., & Flanagan, J. M. (1999). Structural Analysis of the Mechanism of Adenovirus Binding to Its Human Cellular Receptor, CAR. Science. https://doi.org/10.1126/science.286.5444.1579
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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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