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- W61673511 abstract "In this chapter we briefly describe functional and structural properties of the recombinant knob domain of the adenovirus type 5 (Ad5) fiber protein. We were able to demonstrate that this domain forms a trimer in solution and can compete with intact virus for binding to cellular receptors (Henry et al. 1994). We subsequently determined the crystal structure of knob at 1.7 Å resolution (Xia et al. 1994). The knob monomers are β-sandwich structures and are arranged as closely associated trimers in the crystal. We compared sequences of knob domains from different adenovirus serotypes and found patterns of highly conserved and highly variable sequences on the knob surface. We interpreted the conserved regions as probable sites of interaction of the knob ligand with the cellular receptors and the variable regions as antigenic sites which define the structural differences among serotypes.KeywordsCellular ReceptorAdenovirus TypeFiber ProteinTexas Southwestern MedicalAdenovirus SerotypesThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves." @default.
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- W61673511 date "1995-01-01" @default.
- W61673511 modified "2023-09-27" @default.
- W61673511 title "Structure of the Receptor Binding Domain of Adenovirus Type 5 Fiber Protein" @default.
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- W61673511 doi "https://doi.org/10.1007/978-3-642-79496-4_3" @default.
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