Abstract
A synthetic peptide, the N-terminus of hepatitis B virus surface antigen Pre-S1, was studied by twodimensional NMR techniques. A series of1H nuclear magnetic resonance experiments were used to complete the identification of spin systems and sequential assignments of this 28-residue peptide. 157 distance constraints and 55 dihedral angle constraints were obtained. 20 structures with the lowest target function were selected by the distance geometry program DIANA. Energy minimization and the following 100 ps time-averaged restrained molecular dynamics (TR-MD) simulation in aqueous solution were performed for each conformer. After TRMD simulation, three locally convergent regions corresponding to residues 22–31, 36–40, 41–46 were found. The averaged pairwise root-meansquare deviation (RMSD) of backbone atoms for them were (1.71±0.49)A, (0.76 ±0.31)A, (1.05 ± 0.52)A, respectively. Four reverse turns found in these regions, residues 22–25, 37–40, 41–44 and 43–46, correspond to several important antibody binding sites revealed in relevant immunological research.
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References
Milich, D. R., Genetic and molecular basis for T-and B-cell recognition of hepatitis B viral antigens,Immunological Reviews, 1987a, 99: 71.
Neurath, A. R., Kent, S. B. H., Strick, N., Location & chemical synthesis of pre-S gene coded immunodominant epitope of heptitis H virus,Science, 1984, 224: 392.
Xu, L. G., Huang, W. D.,Peptides Biology and Biochemistry, Beijing: Science Press, 1991, 137–138.
Guntert, P., Wuthrich, K., A new procedure for high-quality baseline correction of two-and higher-dimensional NMR spectra,J. Mag. Reson., 1992a, 96: 403.
Bartels, C., Xia, T., Billeter, M. et al., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules,J. Biomol. NMR, 1995, 6: 1.
Guntert, P., Braun, W., Wuthrich, K., Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using program DIANA and the supporting programs CALIBA, HABAS and GLOMSA,J. Mol. Biol., 1991, 217: 517.
Torda, A. E., Scheek, R. M., Van Gunsteren, W. F. et al., Time averaged nuclear overhauser effect distance restraints applied to tendamistat,J. Mol. Biol., 1990, 214: 223.
Nanzer, A. P., Poulsen, F. M., Van Gunsteren, W. F. et al., A reassessment of the structure of chymotrypsin inhibitor 2 (CI-2) using time-averaged NMR restraints,Biochemistry, 1994, 33: 14503.
Van Gunsteren, W. F., Berendsen, H. J. C.,Biomolecular Simulation: The GROMOS96 Manual and User Guide, Groningen: Biomos., 1996.
Nanzer, A. P., Parametrisation of time averaged distance restrains in MD simulations,J. Biol. NMR, 1995, 6: 313.
Wuthrich, K.,NMR of Protein and Nucleic Acids, New York: John Wiley & Sons, 1986.
Dyson, H. J., Rance, M., Houghten, R. A. et al., Folding of immunogenic peptide fragments of proteins in water solution (I) Sequence requirements for the formation of a reverse turn,J. Mol. Biol., 1988a, 201: 161.
Dyson, H. J., Rance, M., Houghten, R. A. et al., Folding of immunogenic peptide fragments of proteins in water solution (II)The nascent helix,J. Mol. Biol., 1988b, 201: 201.
Chandrasekhar, K., Profy, A. T., Dyson, H. J., Solution coformational preferences of immunogenic peptides derived from the principal neutralizing determinant of HIV-1 envelop glycoprotein gp120,Biochemistry, 1991, 30: 9187.
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Project supported in part by the National Foundation Commission of Science and Technology of China.
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Gong, Q., Wu, J., Liu, Q. et al. Solution structure of N-terminal segment of hepatitis B virus surface antigen Pre-S1. Sci. China Ser. C.-Life Sci. 41, 530–541 (1998). https://doi.org/10.1007/BF02882892
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DOI: https://doi.org/10.1007/BF02882892