Biochemistry · 1996 · 59 citations · 16 references
Life SciencesBiochemistryMolecular BiologyCarbohydrate BiochemistryGlycobiologyStructural BiologyGlycan AnalysisGlycan LabelingGlycan StructureGlycan-protein InteractionsN-linked GlycosylationProtein GlycosylationBiological Activity FeaturesCarbohydrate Conformational AnalysisGlycan Structural AnalysisGlycan Structure AnalysisHigh-resolution Solution NmrN-glycan AnalysisNuclear Magnetic Resonance Glycan AnalysisSubunit Association
The conformational properties in solution of the glycans on the alpha subunit of recombinant human chorionic gonadotropin are described, using high-resolution multinuclear NMR studies on uniformly 13C, 15N-enriched recombinant glycoprotein expressed in CHO cells. The glycan important for full biological activity of hCG, namely, that at Asn 52, appears to extend into solution both in the isolated alpha subunit and in complex with the beta subunit. The disposition of this glycan with respect to the protein backbone suggests that glycosylation maintains full biological activity of hCG either by interacting with a lectin-like region of the hCG receptor or by reducing the affinity of the hormone for the hCG receptor and preventing its down-regulation.
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NMR with Proteins and Nucleic Acids
Kurt Wüthrich · Europhysics news · 1986 · 8K citations
Crystal structure of human chorionic gonadotropin
Adrian J. Lapthorn, D. C. Harris, Allison Littlejohn et al. · Nature · 1994 · 938 citations