Glycosylation plays an important role in cell-cell adhesion, ligand-binding, and subcellular recognition. Current approaches for predicting protein glycosylation are primarily based on sequence-derived features, while little work has been done to systematically assess the importance of structural features to glycosylation prediction. Here, we propose a novel bioinformatics method called GlycoMinestruct for improved prediction of human N- and O-linked glycosylation sites by combining sequence and structural features in an integrated computational framework with a two-step feature-selection strategy. Experiments indicated that GlycoMinestruct outperformed NGlycPred, the only predictor that incorporated both sequence and structure features, achieving AUC values of 0.941 and 0.922 for N- and O-linked glycosylation, respectively, on an independent test dataset. We applied GlycoMinestruct to screen the human structural proteome and obtained high-confidence predictions for N- and O-linked glycosylation sites. GlycoMinestruct can be used as a powerful tool to expedite the discovery of glycosylation events and substrates to facilitate hypothesis-driven experimental studies.
Please upload a PDB File
We have investigated the N- and O-linked glycosylation sites for human proteome (20538 structural proteins) with GlycoMinestruct.
The result files can be downloaded here
It is very easy and straightfoward to use the GlycoMinestruct server to make the prediction. All you need to upload is the protein structure file (in. pdb format) to our web server. As GlycoMinestruct will take a while to return the results, please also provide your email address. Once finished, the prediction results will be sent to your nominated email address. Please wait patiently for the prediction result to be returned by our server. Each protein structure may take 5 or more minutes. The table showing the prediction results is demonstrated as follows. The threshold for N-linked and O-linked glycosylation is 0.5.
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