Effects of N-Glycans on Glycoprotein Folding and Protein Dynamics

Amazaki, Yoko; Nguyen, Hien Minh; Okamoto, Ryo; Maki, Yuta; Kajihara, Yasuhiro

doi:10.1007/978-981-13-2158-0_1

Glycobiophysics

2018

DOI: 10.1007/978-981-13-2158-0_1

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Effects of N-Glycans on Glycoprotein Folding and Protein Dynamics

Yoko Amazaki

Hien Minh Nguyen

Ryo Okamoto

et al.

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2020

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Cited by 2 publications

(1 citation statement)

References 35 publications

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“…Glycosylation is a highly prevalent co- or post-translational modification that is bestowed upon a fifth or so of proteins . Glycosylation is known to have diverse consequences, − and articulating the precise effects of glycosylation on the structure and function of proteins is an important ongoing challenge. − We sought to extend extant knowledge in a well-defined context.…”

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confidence: 99%

Structure and Dynamics of N-Glycosylated Human Ribonuclease 1

et al. 2020

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Glycosylation is a common modification that can endow proteins with altered physical and biological properties. Ribonuclease 1 (RNase 1), which is the human homologue of the archetypal enzyme RNase A, undergoes N-linked glycosylation at asparagine residues 34, 76, and 88. We have produced the three individual glycoforms that display the core heptasaccharide, Man5GlcNAc2, and analyzed the structure of each glycoform by using small-angle X-ray scattering along with molecular dynamics simulations. The glycan on Asn34 is relatively compact and rigid, donates hydrogen bonds that “cap” the carbonyl groups at the C-terminus of an α-helix, and enhances protein thermostability. In contrast, the glycan on Asn88 is flexible and can even enter the enzymic active site, hindering catalysis. The N-glycosylation of Asn76 has less pronounced consequences. These data highlight the diverse behaviors of Man5GlcNAc2 pendants and provide a structural underpinning to the functional consequences of protein glycosylation.

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Structure and Dynamics of N-Glycosylated Human Ribonuclease 1

et al. 2020

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Druggability assessment of precursor membrane protein as a target for inhibiting the Zika virus

Mulgaonkar

Wang

King

et al. 2020

Journal of Biomolecular Structure and Dynamics

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Effects of N-Glycans on Glycoprotein Folding and Protein Dynamics

Cited by 2 publications

References 35 publications

Structure and Dynamics of N-Glycosylated Human Ribonuclease 1

Structure and Dynamics of N-Glycosylated Human Ribonuclease 1

Druggability assessment of precursor membrane protein as a target for inhibiting the Zika virus

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