Design of single-layer β-sheets without a hydrophobic core

Nature

Volumn 403, Issue 6768, 2000, Pages 456-460

  Koide, Shohel ^a   Huang, Xiaolin ^a   Link, Karl ^a   Kolde, Akiko ^a   Bu, Zimel ^b   Engelman, Donald M ^b  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN;

ARTICLE; BORRELIA BURGDORFERI; GENETIC ENGINEERING; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; THERMODYNAMICS;

ANTIGENS, SURFACE; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL VACCINES; BORRELIA BURGDORFERI GROUP; LIPOPROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SCATTERING, RADIATION;

BACTERIA (MICROORGANISMS); BORRELIA; BORRELIA BURGDORFERI;

EID: 0034719388     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35000255     Document Type: Article

References (30)

1. Kauzmann, W. Some factors in the interpretation of protein denaturation. Adv. Prot. Chem. 14, 1-63 (1959).
2. Dill, K. A. Dominant forces in protein folding. Biochemistry 29, 7133-7155 (1990).
3. Harbury, P. B., Plecs, J. J., Tidor, B., Alber, T. & Kim, P. S. High-resolution protein design with backbone freedom. Science 282, 1462-1467 (1998).
4. Beasley, J. R. & Hecht, M. H. Protein design: the choice of de novo sequences. J. Biol. Chem. 272, 2031-2034 (1997).
5. Bryson, J. W. et al. Protein design: a hierarchic approach. Science 270, 935-941 (1995).
6. Dahiyat, B. I. & Mayo, S. L. De novo protein design: fully automated sequence selection. Science 278, 82-87 (1997).
7. Li, H., Dunn, J. J., Luft, B. J. & Lawson, C. L. Crystal structure of Lyme disease antigen outer surface protein A complexed with an Fab. Proc. Natl Acad. Sci. USA 94, 3584-3589 (1997).
8. Pham, T.-N., Koide, A. & Koide, S. A stable single-layer β-sheet without a hydrophobic core. Nature Struct. Biol. 5, 115-119 (1998).
9. Bu, Z., Koide, S. & Engelman, D. M. A solution SAXS study of Borrelia burgdorferi OspA, a protein containing a single-layer β-sheet. Protein Sci. 7, 2681-2683 (1998).
10. Pham, T. N. & Koide, S. NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer β-shet. J. Biomol. NMR 11, 407-414 (1998).
11. Koide, S. et al. Multi-step denaturation of Borrelia burgdorferi OspA, a protein containing a single-layer β-sheet. Biochemistry 38, 4757-4767 (1999).
12. 13C chemical-shift data. J. Biomol. NMR 4, 171-180 (1994).
13. 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28, 8972-8979 (1989).
14. Tjandra, N., Garrett, D. S., Gronenbom, A. M., Bax, A. & Clore, G. M. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nature Struct. Biol. 4, 443-449 (1997).
15. 13Cα nuclear spin relaxation. J. Biomol. NMR 9, 287-298 (1997).
16. Kataoka, M., Kuwajima, K., Tokunaga, F. & Goto, Y. Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering. Protein Sci. 6, 422-430 (1997).
17. Lattman, E. E. Small angle scattering studies of protein folding. Curr. Opin. Struct. Biol. 4, 87-92 (1994).
18. Englander, S. W. & Kallenbach, N. R. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 6, 521-655 (1984).
19. Hughson, F. M., Wright, P. E. & Baldwin, R. L. Structural characterization of a partly folded apomyoglobin intermediate. Science 249, 1544-1548 (1990).
20. Myers, J. K., Pace, C. N. & Scholtz, J. M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148 (1995).
21. Lacroix, E., Kortemme, T., de la Paz, M. L. & Serrano, L. The design of linear peptides that fold as monomeric beta-sheet structures. Curr. Opin. Struct. Biol. 9, 487-493 (1999).
22. Macias, M. J. et al. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 382, 646-649 (1996).
23. Koepf, E. K., Petrassi, H. M., Sudol, M. & Kelly, J. W. WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded state. Protein Sci. 8, 841-853 (1999).
24. Fink, A. L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold. Des. 3, R9-R23 (1998).
25. Kelly, J. W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101-106 (1998).
26. Perutz, M. F., Johnson, T., Suzuki, M. & Finch, J. T. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl Acad. Sci. USA 91, 5355-5358 (1994).
27. Clore, G. M. & Gronenborn, A. M. Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Prog. NMR Spectrosc. 23, 43-92 (1991).
28. 15N NMR relaxation. Biochemistry 33, 5984-6003 (1994).
29. Brunger, A. T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
30. Kraulis, P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950 (1991).