The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability
作者： S. R. Hanson , E. K. Culyba , T.-L. Hsu , C.-H. Wong , J. W. Kelly
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摘要: The folding energetics of the mono-N-glycosylated adhesion domain human immune cell receptor cluster differentiation 2 (hCD2ad) were studied systematically to understand influence N-glycan on energy landscape. Fully elaborated structures accelerate by 4-fold and stabilize β-sandwich structure 3.1 kcal/mol, relative nonglycosylated protein. N-glycan's first saccharide unit accounts for entire acceleration 2/3 native state stabilization. remaining third stabilization is derived from next units. Thus, conserved N-linked triose core, ManGlcNAc2, improves both kinetics thermodynamics protein folding. decreased activation barrier conferred N-glycosylation provide a powerful potentially general mechanism enhancing in secretory pathway.
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