Glycoproteins: Glycan presentation and protein-fold stability

Structure

Volumn 7, Issue 7, 1999, Pages

  Wormald, Mark R ^a   Dwek, Raymond A ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN DERIVATIVE; GLYCOPROTEIN;

HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SHORT SURVEY; STRUCTURE ANALYSIS;

EID: 0033566020     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80095-1     Document Type: Review

References (35)

1. Petrescu, A.J., Petrescu, S.M., Dwek, R.A. & Wormald, M. R. (1999). A statistical analysis of N- and O-glycan linkage conformations from crystallographic data. Glycobiology 9, 343-352.
2. 13C) enriched oligosaccharides. Glycobiology 8, 147-153.
3. Woods, R. J. (1998). Computational carbohydrate chemistry: What theoretical methods can tell us. Glycoconjugate J. 15, 209-216.
4. Petrescu, A.J., et al., & Wormald, M.R. (1997). The solution NMR structure of glucosylated N-glycans involved in the early stages of glycoprotein biosynthesis and folding. EMBO J. 16, 4302-4310.
5. x group. Biochem. Biophys. Res. Commun. 180, 1214-1221.
6. Rutherford, T.J., Neville, D.C. & Homans, S.W. (1995). Influence of the extent of branching on solution conformations of complex oligosaccharides: A molecular dynamics and NMR study of a penta-antennary "bisected" N-glycan. Biochemistry 34, 14131-14137.
7. Woods, R.J., Pathiaseril, A., Wormald, M.R., Edge, C.J. & Dwek, R.A. (1998). The high degree of internal flexibility observed for an oligomannose oligosaccharide is not reproduced in the overall topology of the molecule. Eur. J. Biochem. 258, 372-386.
8. Wormald, M.R., et al., & Dwek, R.A. (1991) The conformational effects of N-glycosylation on the tailpiece from serum IgM. Eur. J. Biochem. 198, 131-139.
9. 2O. J. Biol. Chem. 269, 3331-3338.
10. Imberty, A. & Perez, S. (1995). Stereochemistry of the N-glycosylation sites in glycoproteins. Prof. Eng. 8, 699-709.
11. Imperiali, B. & Rickert, K.W. (1995). Conformational implications of asparagine-linked glycosylation. Proc. Natl Acad Sci. USA 92, 97-101.
12. Lommerse, J.P., Kroon Batenburg, L.M., Kroon, J., Kamerling, J.P. & Vliegenthart, J.F. (1995). Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis. J. Biomol. NMR 6, 79-94.
13. Live, D.H., Kumar, R.A., Beebe, X. & Danishefsky, S.J. (1996). Conformational influences of glycosylation of a peptide: A possible model for the effect of glycosylation on the rate of protein folding. Proc. Natl Acad. Sci. USA 93, 12759-12761.
14. Huang, X., et al., & Garrity, R.R. (1997). Glycosylation affects both the three-dimensional structure and antibody binding properties of the HIV-1 IIIB GP120 peptide RP135. Biochemistry 36, 10846-10856.
15. Gerken, T.A., Butenhof, K.J. & Shogren, R. (1989). Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: Carbon-13 NMR studies of ovine submaxillary mucin. Biochemistry 28, 5536-5543.
16. Bodian, D.L., Jones, E.Y., Harlos, K., Stuart, D.I. & Davis, S.J. (1994). Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure 2, 755-766.
17. Driscoll, P.C., Cyster, J.G., Campbell, I.D. & Williams, A.F. (1991 ). Structure of domain 1 of rat T lymphocyte CD2 antigen. Nature 353, 762-765.
18. 1H resonance assignments and secondary structure of the 13.6 kDa glycosylated adhesion domain of human CD2. Biochemistry 32, 10995-11006.
19. Wyss, D.F., Choi, J.S. & Wagner, G. (1995). Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein. Biochemistry 34, 1622-1634.
20. Wyss, D.F., et al., & Wagner, G. (1995). Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Science 269, 1273-1278.
21. Williams, R.L., Greene, S.M. & McPherson, A. (1987). The crystal structure of ribonuclease B at 2.5 Å resolution. J. Biol. Chem. 262, 16020-16031.
22. Joao, H.C. & Dwek, R.A. (1993). Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its individual glycoforms. Eur. J. Biochem. 218, 239-244.
23. Pao, Y.-L. (1998). Conformational and Dynamic Studies of the Influence of Glycosylation on Peptides and Proteins, D. Phil., University of Oxford.
24. Lapthorn, A.J., et al., & Isaacs, N.W. (1994). Crystal structure of human chorionic gonadotropin. Nature 369, 455-461.
25. De Beer, T., et al., & Vliegenthart, J.F. (1996). NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit. Eur. J. Biochem. 241, 229-242.
26. van Zuylen, C.W., Kamerling, J.P. & Vliegenthart, J.F. (1997). Glycosylation beyond the Asn78-linked GlcNAc residue has a significant enhancing effect on the stability of the alpha subunit of human chorionic gonadotropin. Biochem. Biophys. Res. Commun. 232, 117-120.
27. 15N-enriched recombinant human chorionic gonadotropin. Biochemistry 35, 8815-8823.
28. van Zuylen, C.W., et al., & Vliegenthart, J.F. (1998). Mobilities of the inner three core residues and the Man(alpha 1-6) branch of the glycan at Asn78 of the alpha-subunit of human chorionic gonadotropin are restricted by the protein. Biochemistry 37, 1933-1940.
29. Deisenhofer, J., Colman, P.M., Epp, O. & Huber, R. (1976). Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 Å resolution. Hoppe- Seyler's Z. Physiol. Chem. 357, 1421-1434.
30. 13C nuclear magnetic resonance spectroscopy. Mol. Immunol. 16, 435-436.
31. Wormald, M.R., Rudd, P.M., Harvey, D.J., Chang, S.C., Scragg, I.G. & Dwek, R.A. (1997). Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry 36, 1370-1380.
32. Corper, A.L., et al., & Sutton, B.J. (1997). Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction. Nat. Struct. Biol. 4, 374-381.
33. Deisenhofer, J. (1981 ). Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9 and 2.8 Å resolution. Biochemistry 20, 2361-2370.
34. Joao, H.C., Scragg, I.G. & Dwek, R.A. (1992). Effects of glycosylation on protein conformation and amide proton exchange rates in RNase B. FEBS Lett. 307, 343-346.
35. Brown, M.J. & Shaw, S. (1999). T-cell activation: Interplay at the interface. Curr. Biol. 9, R26-R28.