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Home > Mathematics and Science Textbooks > Science: general issues > Enhanced Aromatic Sequons in Turns Reliably Stabilize N-Linked Glycoprotein Native States.
Enhanced Aromatic Sequons in Turns Reliably Stabilize N-Linked Glycoprotein Native States.

Enhanced Aromatic Sequons in Turns Reliably Stabilize N-Linked Glycoprotein Native States.


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About the Book

Nearly 1/3 of the human proteome traverses the cellular secretory pathway. Most of these proteins are N-glycosylated at Asn within the Asn1-Xxx 2-Thr/Ser3 sequon. Nglycosylation can increase the stability of proteins, but the molecular basis for this is incompletely understood. We first studied the role of the highly conserved N-glycan structure in the folding energetics of the adhesion domain of the human immune cell receptor CD2 (HsCD2ad) to systematically understand the influence of N-glycans on folding landscapes. Fully elaborated N-glycan structures accelerate folding by 4-fold and stabilize the structure by 3.1 kcal/mol, relative to the non-glycosylated protein. The Nglycan's first saccharide unit accounts for the all of the acceleration of folding and twothirds of the native state stabilization. The remaining stabilization is derived from the next two saccharide units (ManGlcNAc). We then used the structurally homologous rat ortholog of HsCD2ad (RnCD2ad) to study the role of protein-glycan contacts in Nglycan- based native state stabilization. Here we show that placement of a Phe two or three residues prior to a glycosylated Asn in a reverse turn context facilitates interactions between the aromatic side-chain, the first N-acetylglucosamine (GlcNAc) of the glycan and the Thr side chain. Engineering this "enhanced aromatic sequon" into reverse turns in three different glycosylation-naive proteins stabilizes their native states by up to -0.7 to - 2.5 kcal/mol, substantially slows unfolding and increases glycosylation efficiency. These results enable the design of glycoproteins, including therapeutics, with predictable effects on stability, which is currently a challenge.


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Product Details
  • ISBN-13: 9781244675230
  • Publisher: Proquest, Umi Dissertation Publishing
  • Publisher Imprint: Proquest, Umi Dissertation Publishing
  • Height: 254 mm
  • Weight: 367 gr
  • ISBN-10: 1244675237
  • Publisher Date: 30 Sep 2011
  • Binding: Paperback
  • Spine Width: 12 mm
  • Width: 203 mm


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Enhanced Aromatic Sequons in Turns Reliably Stabilize N-Linked Glycoprotein Native States.
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Enhanced Aromatic Sequons in Turns Reliably Stabilize N-Linked Glycoprotein Native States.
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