Comparative ligand structural analytics illustrated on variably glycosylated MUC1 antigen-antibody binding.

ABSTRACT: When faced with the investigation of the preferential binding of a series of ligands against a known target, the solution is not always evident from single structure analysis. An ensemble of structures generated from computer simulations is valuable; however, visual analysis of the extensive structural data can be overwhelming. Rapid analysis of trajectory data, with tools available in the Galaxy platform, can be used to understand key features and compare differences that inform the preferential ligand structure that favors binding. We illustrate this informatics approach by investigating the in-silico binding of a peptide and glycopeptide epitope of the glycoprotein Mucin 1 (MUC1) binding with the antibody AR20.5. To study the binding, we performed molecular dynamics simulations using Op

SUBMITTER: Barnett CB 

PROVIDER: S-EPMC7590620 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature