Structure of adenovirus fibre. II. Morphology of single fibres

J Mol Biol. 1990 Oct 20;215(4):589-96. doi: 10.1016/S0022-2836(05)80170-6.


Adenovirus type 2 fibres in crystals appear to be significantly longer than found previously (accompanying paper). We therefore examined isolated fibre by electron microscopy and measured a length of 370 A, consistent with the length found in the crystals. The specific N-terminal structure of the fibre caused a heterogeneity in the length that may at least partially explain the values of 280 to 310 A published previously. Green et al. described a 15 amino acid repeat in the primary structure of the shaft of the fibre thought to be associated with the specific three-dimensional folding of the shaft. We compared the adenovirus type 2 (with 22 repeats) and type 3 (with 6 repeats) fibre lengths and derived a contribution of 13.2 A to the length of the shaft per 15 amino acid repeat. Specific morphological features of the fibre are discussed in relation to its amino acid sequence.

Publication types

  • Comparative Study

MeSH terms

  • Capsid / genetics
  • Capsid / ultrastructure*
  • Capsid Proteins*
  • Electrophoresis, Polyacrylamide Gel
  • Genetic Variation
  • HeLa Cells
  • Humans
  • Molecular Weight
  • Repetitive Sequences, Nucleic Acid
  • Solutions


  • Capsid Proteins
  • Solutions
  • hexon capsid protein, Adenovirus