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. 2005 Jul 1;33(Web Server issue):W214-9.
doi: 10.1093/nar/gki385.

GlyProt: in silico glycosylation of proteins

Andreas Bohne-Lang  1 , Claus-Wilhelm von der Lieth
Affiliations

GlyProt: in silico glycosylation of proteins

Andreas Bohne-Lang et al. Nucleic Acids Res. .

Abstract

GlyProt (http://www.glycosciences.de/glyprot/) is a web-based tool that enables meaningful N-glycan conformations to be attached to all the spatially accessible potential N-glycosylation sites of a known three-dimensional (3D) protein structure. The probabilities of physicochemical properties such as mass, accessible surface and radius of gyration are calculated. The purpose of this service is to provide rapid access to reliable 3D models of glycoproteins, which can subsequently be refined by using more elaborate simulations and validated by comparing the generated models with experimental data.

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Figures

Figure 1
Figure 1
Dataflow of GlyProt.
Figure 2
Figure 2
Statistical analysis of the PDB for torsion angles determining the orientation of the glycan moiety relative to the protein.
Figure 3
Figure 3
Statistical analysis of the PDB for glycosidic torsion angles determining the conformation of the N-glycan core.
Figure 4
Figure 4
Input spreadsheet (top) used to query the database, which contains >1000 3D structures of N-glycans (bottom). The user indicates the desired glycoform by checking the corresponding selection box.
Figure 5
Figure 5
User interface (top) to select the desired glycoform for each gycosylation site. Visualization (bottom) of the constructed glycoprotein. The protein part is given as a cartoon representation; the glycan part as a spacefill model.
See this image and copyright information in PMC

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