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Three-Dimensional Structure of the Adenovirus Major Coat Protein Hexon

Roberts, Michael M., White, Janice L., Grütter, Markus G., Burnett, Roger M.·1986·Science

Abstract

The three-dimensional crystal structure of the adenovirus major coat protein is presented. Adenovirus type 2 hexon, at 967 residues, is now the longest polypeptide whose structure has been determined crystallographically. Taken with our model for hexon packing, which positions the 240 trimeric hexons in the capsid, the structure defines 60% of the protein within the 150 × 10 6 dalton virion. The assembly provides the first details of a DNA-containing animal virus that is 20 times larger than the spherical RNA viruses previously described. Unexpectedly, the hexon subunit contains two similar β-barrels whose topology is identical to those of the spherical RNA viruses, but whose architectural role in adenovirus is very different. The hexon structure reveals several distinctive features related to its function as a stable protective coat, and shows that the type-specific immunological determinants are restricted to the virion surface.

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Metadata

Authors
Roberts, M. M., White, J. L., Grütter, M. G., & Burnett, R. M.
Venue
Science
Published
1986-05-30
Volume
232
Issue
4754
Pages
1148-1151
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1975725195
Cited by
247
References
0
FWCI
15.74
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Three-Dimensional Structure of the Adenovirus Major Coat Protein Hexon. https://app.cochat.ai/papers/10.1126/science.3704642
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Roberts, M. M., White, J. L., Grütter, M. G., & Burnett, R. M. (1986). Three-Dimensional Structure of the Adenovirus Major Coat Protein Hexon. Science. https://doi.org/10.1126/science.3704642

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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.