FIG 1.

Positions of potential N-linked glycosylation sites in PrV gH. (A) The primary translation product of PrV gH (686 aa) is schematically shown. The first amino acids of the predicted signal peptide (SP), the ectodomain parts (I to IV), the transmembrane domain (TMD), and the cytoplasmic domain (CD), as well the modified asparagine (N) residues, are indicated. (B) Crystal structure of the gH core fragment (aa 107 to 639) (20). The N and C termini are labeled. In domain II, the fence (dark blue) and the syntaxin-like bundle (SLB) (light blue) are indicated. Domain III is colored yellow and domain IV red, with the flap highlighted in blue. Predicted glycosylation sites at N162, N542, and N627 are indicated by green spheres. N604 lies within a flexible region (dashed green line), which was not solved in the crystal structure. N77 was not included in the construct used for crystallization. The image was generated using the UCSF Chimera package (version 1.11.2) (65).