 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
journal menu
![[Figure 4]](ir5003fig4mag.jpg)
|
|
Figure 4
Distinct binding epitopes of MCPyV and BKPyV VP1 in complex with the GD3 glycan. (a) GD3 reference spectrum (top), BKPyV and MCPyV VP1 STD-NMR difference spectra (second and third from top) and TOCSY spectra of individual pyranoses in the GD3 tetrasaccharide, labelled with SNFG representations as in Fig. 2 ![[link]](../../../../../../logos/arrows/f_arr.gif) . TOCSY spectra for both anomeric forms of the reducing-end Glc ring are shown (bottom and second from bottom). Impurities are represented by asterisks. Selected resonances in the TOCSY spectra are labelled. The H3–H6 proton resonances of the Neu5Acα2–3 ring and the H1 and H4 proton resonances of the Gal ring are clearly recognizable in the MCPyV VP1 STD difference spectrum (at 4.48 and 3.90 p.p.m., respectively). The epitope seen in the BKPyV VP1 difference spectrum, in contrast, mostly includes resonances of both Neu5Ac rings. The truncated peaks at 2 p.p.m. (framed) belong to the Neu5Ac methyl groups, which are also shown in full in (b). HDO and methyl-group signals were truncated. More detailed assignments of both STD difference spectra can be found in Neu et al. (2012, 2013). NMR spectra were recorded at 283 K and re-referenced to 298 K; the STD saturation time was 2 s. (c) 3D-SNFG (top, in grey) representation of the GD3 epitope as bound in the MCPyV VP1–GD3 crystal structure (bottom, with the GD3 middle disaccharide in light orange; Neu et al., 2012). Aliphatic H atoms were added to the crystal structure in PyMOL. |
![[Figure 4]](ir5003fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
access
