C-Mannosylation Enhances the Structural Stability of Human RNase 2
Martin Frank, Daniela Beccati, Bas R. Leeflang, Johannes F.G. Vliegenthart
Abstract
is the most abundant. However, for native RNase 2, molecular dynamics and NMR studies revealed that the mannopyranosyl residue favors a specific conformation, which optimally stabilizes the protein fold through a network of hydrogen bonds and which leads to a significant reduction of the protein dynamics on the microsecond timescale. Our findings contribute to the understanding of the biological role of C-mannosylation.
Topics & Concepts
RNase PChemistryAngiogeninMolecular dynamicsTryptophanGlycosylationStereochemistryProtein structureResidue (chemistry)MoietyNuclear magnetic resonance spectroscopyAmino acidBiochemistryComputational chemistryBiologyRNAGeneAngiogenesisCancer researchGlycosylation and Glycoproteins ResearchCarbohydrate Chemistry and SynthesisRNA and protein synthesis mechanisms