The adenovirus hexon protein. The primary structure of the polypeptide and its correlation with the hexon gene

The primary structure of the adenovirus hexon polypeptide has been determined by amino acid sequence studies of peptides from all regions of the molecule combined with sequence analysis of selected areas of its gene. The sequence presented contains 966 unique amino acid residues. Overlapping peptide...

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Bibliographic Details
Published in:The Journal of biological chemistry 1981-06, Vol.256 (12), p.6181-6186
Main Authors: H Jörnvall, G Akusjärvi, P Aleström, H von Bahr-Lindström, U Pettersson, E Appella, A V Fowler, L Philipson
Format: Article
Language:English
Subjects:
adenovirus (human) 2
Adenoviruses, Human - analysis
Amino Acid Sequence
Base Sequence
Capsid - genetics
Capsid Proteins
Cyanogen Bromide
DNA Restriction Enzymes
DNA, Viral
gene mapping
hexons
Peptide Fragments
proteins
Viral Proteins - genetics
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Summary:The primary structure of the adenovirus hexon polypeptide has been determined by amino acid sequence studies of peptides from all regions of the molecule combined with sequence analysis of selected areas of its gene. The sequence presented contains 966 unique amino acid residues. Overlapping peptides recovered from CNBr cleavage and from digestions with proteolytic enzymes were analyzed, as well as DNA segments around sites for restriction endonucleases in the hexon gene. The primary structure is in good agreement with the total composition of the protein, with the compositions of individual CNBr fragments, and with known locations of restriction enzyme cleavage sites in the gene. Distinct regions of internal homology do not occur in the structure. The entire hexon polypeptide is encoded by a contiguous DNA sequence without intervening sequences.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)69145-3