Crystal structure of the receptor-binding domain of adenovirus type 5 fiberprotein at 1.7 Å resolution

Di Xia, Lynda J. Henry, Robert D. Gerard, Johann Deisenhofer

Research output: Contribution to journalArticlepeer-review

247 Scopus citations


Background: Adenoviral infection begins with the binding of virion to the surface of host cells. Specific attachment is achieved through interactions between host-cell receptors and the adenovirus fiber protein and is mediated by the globular carboxy-terminal domain of the adenovirus fiber protein, termed the carboxy-terminal knob domain. Results The crystal structure of the carboxy-terminal knob domain of the adenovirus type 5 (Ad5) fiber protein has been determined at 1.7 Å resolution. Each knob monomer forms an eight-stranded antiparallel β-sandwich structure. In the crystal lattice, the knob monomers form closely interacting trimers which possess a deep surface depression centered around the three-fold molecular symmetry axis and three symmetry-related valleys. Conclusion The amino acid residues lining the wall of the central surface depression and the three symmetry-related floors of the valleys are strictly conserved in the knob domains of Ad5 and adenovirus type 2 (Ad2) fiber proteins, which share the same cellular receptor. The β-sandwich structure of the knob monomer demonstrates a unique folding topology which is different from that of other known antiparallel β-sandwich structures. The large buried surface area and numerous polar interactions in the trimer indicate that this form of the knob protein is predominant in solution, suggesting a possible assembly pathway for the native fiber protein.

Original languageEnglish (US)
Pages (from-to)1259-1270
Number of pages12
Issue number12
StatePublished - Dec 1994


  • adenovirus fiber protein
  • adenovirus type 5
  • receptor-binding protein
  • viral assembly
  • virus-host interaction

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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