Defining the Specificity of Carbohydrate-Protein Interactions by Quantifying Functional Group Contributions.

ABSTRACT: Protein-carbohydrate interactions are significant in a wide range of biological processes, disruption of which has been implicated in many different diseases. The capability of glycan-binding proteins (GBPs) to specifically bind to the corresponding glycans allows GBPs to be utilized in glycan biomarker detection or conversely to serve as targets for therapeutic intervention. However, understanding the structural origins of GBP specificity has proven to be challenging due to their typically low binding affinities (mM) and their potential to display broad or complex specificities. Here we perform molecular dynamics (MD) simulations and post-MD energy analyses with the Poisson-Boltzmann and generalized Born solvent models (MM-PB/GBSA) of the Erythrina cristagalli lectin (ECL) with its known

SUBMITTER: Sood A 

PROVIDER: S-EPMC6442460 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature