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Science 30 May 1986:
Vol. 232. no. 4754, pp. 1148 - 1151
DOI: 10.1126/science.3704642
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Articles

Science, Vol 232, Issue 4754, 1148-1151
Copyright © 1986 by American Association for the Advancement of Science

articles

Three-dimensional structure of the adenovirus major coat protein hexon

MM Roberts, JL White, MG Grutter, and RM Burnett

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 X 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 beta-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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