core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 106; no. 9; pp. 3131 - 3136
• Main Authors: Hanson, Sarah R, Culyba, Elizabeth K, Hsu, Tsui-Ling, Wong, Chi-Huey, Kelly, Jeffery W, Powers, Evan T
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 03.03.2009; National Acad Sciences
• Subjects: adhesion; Amino acids; Animals; Biochemistry; Biological Sciences; CD2 Antigens - chemistry; CD2 Antigens - genetics; CD2 Antigens - metabolism; Cells; Circular Dichroism; energy; Free energy; Glycoproteins; Glycoproteins - chemistry; Glycoproteins - metabolism; Glycosylation; Humans; Immune system; Kinetics; landscapes; Models, Molecular; Mutation - genetics; Oligosaccharides; Physical Sciences; Polysaccharides; Protein Folding; Protein Stability; Protein Structure, Tertiary; Rats; Renovations; Surface areas; Thermodynamics; trisaccharides; Trisaccharides - chemistry; Trisaccharides - metabolism

The folding energetics of the mono-N-glycosylated adhesion domain of the human immune cell receptor cluster of differentiation 2 (hCD2ad) were studied systematically to understand the influence of the N-glycan on the folding energy landscape. Fully elaborated N-glycan structures accelerate folding b...