|
Figure 1.
FIG. 1. A, schematic representation of the domain structure
of the proteins described in this study. 1, the stable
adenovirus fiber fragment (fiber residues 319-582). Residues
belonging to the shaft domain (Val319-Gly392) are symbolized
with a rectangle, and residues belonging to the globular head
(Leu399-Glu582) are symbolized with a circle. Residues 393-398
(Asn-Lys-Asn-Asp-Asp-Lys) form the linker that connects the two
parts and are drawn in italics. 2, the chimeric protein that
comprises the fibritin foldon domain (fibritin residues
Gly457-Leu483, oval shape) fused to the C terminus of the shaft
domain with use of the natural linker between the two domains.
To avoid confusion, the numbers corresponding to the fibritin
residues are underlined. The residues Gly-Ser, highlighted in
bold, are not part of the coding sequence and are introduced as
a result of the cloning strategy. 3, the chimeric protein
carrying the foldon domain at the C-terminal end of the shaft
domain without the use of the natural linker sequence. 4, the
chimeric protein carrying the foldon domain at the N-terminal
end of the shaft domain. The residues Gly-Ser-Gly, highlighted
in bold, do not belong to the coding sequence and are introduced
as a result of the cloning strategy. B, amino acid sequences of
the fiber shaft residues 319-392 and of the fibritin foldon
residues 457-483. The fiber shaft sequence repeat numbers
(repeats 18-22 according to Ref. 9) are indicated on the left.
The repeats are not aligned.
|
