Tertiary structure in N-linked oligosaccharides.

Distance constraints derived from two-dimensional nuclear Overhauser effect measurements have been used to define the orientation of the Man alpha 1-3Man beta linkage in seven different N-linked oligosaccharides, all containing the common pentasaccharide core Man alpha 1-6(Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4GlcNAc. Conformational invariance of the Man alpha 1-3Man beta linkage was found for those structures bearing substitutions on the Man alpha 1-3Man beta antenna. However, the presence of either a GlcNAc residue in the beta 1-4 linkage to Man beta ("bisecting GlcNAc") or a xylose residue in the beta 1-2 linkage to Man beta of the trimannosyl core was found to generate conformational transitions that were similar. These transitions were accompanied by characteristic chemical shift perturbations of proton resonances in the vicinity of the Man alpha 1-3Man beta linkage. Molecular orbital energy calculations suggest that the conformational transition between the unsubstituted and substituted cores arises from energetic constraints in the vicinity of the Man alpha 1-3Man beta linkage, rather than specific long-range interactions. These data taken together with our previous results on the Man alpha 1-6Man beta linkage [Homans, S. W., Dwek R. A., Boyd, J., Mahmoudian, M., Richards, W. G., & Rademacher, T. W. (1986) Biochemistry 25, 6342] allow us to discuss the consequences of the modulation of oligosaccharide solution conformations.

[1]  R. Dwek,et al.  The β1 → 2‐d‐xylose and α1 → 3‐l‐fucose substituted N‐linked oligosaccharides from Erythrina cristagalli lectin , 1987 .

[2]  A. Bax,et al.  Direct identification of relayed nuclear overhauser effects , 1986 .

[3]  W. Richards,et al.  Conformational transitions in N-linked oligosaccharides. , 1986, Biochemistry.

[4]  G. Hart,et al.  Influence of quaternary structure on glycosylation. Differential subunit association affects the site-specific glycosylation of the common beta-chain from Mac-1 and LFA-1. , 1986, The Journal of biological chemistry.

[5]  J. Keeler,et al.  “False” transverse NOE enhancements in CAMELSPIN spectra , 1986 .

[6]  H. Schachter,et al.  Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. , 1986, Biochemistry and cell biology = Biochimie et biologie cellulaire.

[7]  D. G. Davis,et al.  Practical aspects of two-dimensional transverse NOE spectroscopy , 1985 .

[8]  R. Ryan,et al.  Inhibition of adenylyl cyclase activity in rat corpora luteal tissue by glycopeptides of human chorionic gonadotropin and the alpha-subunit of human chorionic gonadotropin. , 1985, Biochemistry.

[9]  R. Dwek,et al.  Multiple-step relayed correlation spectroscopy: sequential resonance assignments in oligosaccharides. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[10]  M. Klein,et al.  Possible role for peptide-oligosaccharide interactions in differential oligosaccharide processing at asparagine-107 of the light chain and asparagine-297 of the heavy chain in a monoclonal IgG1 kappa. , 1984, Biochemistry.

[11]  B. Meyer,et al.  Konformationsanalyse. XXIV: Bestimmung der Konformationen von Tri- und Tetrasaccharid-Sequenzen der Core-Struktur von N-Glycoproteinen. Problem der (1→6)-glycosidischen Bindung , 1984 .

[12]  A. Kobata,et al.  Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides. , 1983, The Journal of biological chemistry.

[13]  R. Dwek,et al.  Solution conformation of biantennary complex type oligosaccharides , 1983 .

[14]  J. Brisson,et al.  Solution conformation of asparagine-linked oligosaccharides: alpha(1-6)-linked moiety. , 1983, Biochemistry.

[15]  J. Brisson,et al.  Solution conformation of asparagine-linked oligosaccharides: alpha(1-2)-, alpha(1-3)-, beta(1-2)-, and beta(1-4)-linked units. , 1983, Biochemistry.

[16]  R. Dwek,et al.  Solution conformation of the biantennary N‐linked oligosaccharide of human serotransferrin using 1H NMR nuclear Overhauser effect measurements , 1982, FEBS letters.

[17]  K. Bock,et al.  The preferred conformation of oligosaccharides derived from the complex-type carbohydrate portions of glycoproteins. , 1982, European journal of biochemistry.

[18]  D. States,et al.  A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants☆ , 1982 .

[19]  K Wüthrich,et al.  Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance. , 1982, Journal of molecular biology.

[20]  N. Sharon,et al.  Primary structure of the carbohydrate chain of soybean agglutinin. A reinvestigation by high resolution 1H NMR spectroscopy. , 1981, The Journal of biological chemistry.

[21]  Richard R. Ernst,et al.  Coherence transfer in the rotating frame , 1979 .

[22]  K. Wüthrich,et al.  NOE difference spectroscopy: A novel method for observing individual multiplets in proton NMR spectra of biological macromolecules , 1978 .

[23]  A. Gronenborn,et al.  Assessment of errors involved in the determination of interproton distance ratios and distances by means of one- and two-dimensional NOE measurements , 1985 .