Effect of glycosylation on structure and dynamics of MHC class I glycoprotein: A molecular dynamics study

摘要: Complex carbohydrates linked to glycoproteins are recently being implicated play a variety of biological roles. The lack well-resolved crystallographic coordinates the makes it difficult assess contributions glycan chain on protein structure and dynamics. We have modeled two different oligosaccharides NeuNAc2Gal3Man3GlcNAc5Fuc Man3GlcNAc4 generate glycosylation variants major histocompatibility complex (MHC) class I glycoprotein. Molecular dynamics simulations isolated fourteen- seven-residue been done in vacuo solution. glycoforms MHC simulated solution free as well peptide-bound form. Good agreement between calculated conformations conjugated forms average obtained from x-ray or NMR data was observed for most glycosidic linkages. These molecular chains glycoconjugates reveal details conformational flexibility chains; they also provide atomic level protein-carbohydrate interactions effect ligand binding carbohydrate It found that though there is some linkages oligosaccharides, protein-conjugated form adopt more restricted conformations. protrude out into solvent might hinder lateral association proteins. presence bulky does not affect backbone fold but induces local changes has noted extent depends upon nature attached chain. do appear influence peptide property directly, may stabilize residues involved binding.