Proline affects oligomerization of a coiled coil by inducing a kink in a long helix

Journal of Structural Biology

Volumn 128, Issue 3, 1999, Pages 270-279

  Chang, Ding Kwo ^a   Cheng, Shu Fang ^a   Trivedi, Vishwa Deo ^a   Lin, Keng Lung ^a  

^a INSTITUTE OF CHEMISTRY   (Taiwan)

Author keywords

Aggregation number; Coiled coil; Fusogenic activity; Kink in helix

Indexed keywords

MEMBRANE PROTEIN; PROLINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL REACTION KINETICS; CIRCULAR DICHROISM; LIGHT SCATTERING; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; THERMOSTABILITY; X RAY DIFFRACTION;

EID: 0033619917     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1999.4182     Document Type: Article

References (37)

1. Barlow D. J., Thornton J. M. Helix geometry in proteins. J. Mol. Biol. 201:1988;601-619.
2. Bartels C., Xia T., Billeter M., Güntert P., Wüthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR. 6:1995;1-10.
3. Bernstein H. B., Tucker S. P., Kar S. R., McPherson S. A., McPherson D. T., Dubay J. W., Lebowitz J., Compans R. W., Hunter E. Oligomerization of the hydrophobic heptat repeat of gp41. J. Virol. 69:1995;2745-2750.
4. Brandts J. F., Halvorson H. R., Brennan M. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry. 14:1975;4953-4963.
5. Caffrey M., Cai M., Kaufman J., Stahl S. J., Wingfield P. T., Covell D. G., Gronenborn A. M., Clore G. M. Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41. EMBO J. 17:1998;4572-4584.
6. Chan D. C., Kim P. S. HIV entry and its inhibition. Cell. 93:1998;681-684.
7. Chan D. C., Fass D., Berger J. M., Kim P. S. Core structure of gp41 from HIV-1 envelope glycoprotein. Cell. 89:1997;263-273.
8. Chang D. K., Cheng S. F., Chien W. J. The amino-terminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface. J. Virol. 71:1997;6593-6602.
9. Chen S. S. L. Functional role of the zipper motif region of human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 68:1994;2002-2010.
10. Chen S. S. L., Lee C. N., Lee W.-R., McIntosh K., Lee T. H. Mutational analysis of leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein. J. Virol. 67:1993;3615-3619.
11. Chen S. S. L., Lee S. F., Hao H. J., Chuang C. H. Mutation in the leucine zipper-like heptad repeat sequence of HIV-1 gp41 dominantly interfere with wild type virus infectivity. J. Virol. 72:1998;4765-4774.
12. Cheng S. F., Chang D. K. Proline-induced kink in a helix arises primarily from dihedral angle energy: A molecular dynamics simulation on alamethicin. Chem. Phys. Lett. 301:1999;453-457.
13. Delwart E. L., Mosialos G., Gilmore T. Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat. AIDS Res. Hum. Retroviruses. 6:1990;703-706.
14. Dubay J. W., Roberts S. J., Brody B., Hunter E. Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66:1992;4748-4756.
15. 1H NMR. Evidence for conformational heterogeneity in a voltage-gated peptide. Biochemistry. 33:1994;4036-4045.
16. Furuta R., Wild C. T., Weng Y., Weiss C. D. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 3:1998;465-469.
17. Gallaher W. R. Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses. Cell. 85:1996;477-478.
18. Gerwert K., Hess B., Engelhard M. Proline residues undergo structural changes during proton pumping. FEBS Lett. 261:1990;449-454.
19. Gibbs N., Sessions R. B., Williams P. B., Dempsey C. E. Helix bending in alamethicin: Molecular dynamics simulations and amide hydrogen exchange in methanol. Biophys. J. 72:1997;2490-2495.
20. Havel T. F., Kuntz I. D., Crippen G. M. The theory and practice of distance geometry. Bull. Math. Biol. 45:1983;665-720.
21. Kouzarides T., Ziff E. The role of leucine zipper in the fos-jun interaction. Nature. 336:1988;646-651.
22. Kreis T., Lodish H. Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface. Cell. 46:1986;929-937.
23. Landschulz W. H., Johnson P. F., McKnight S. L. The leucine zipper: A hypothetical structure common to a new class of DNA binding proteins. Science. 240:1988;1759-1764.
24. Li S. C., Goto N. K., Williams K. A., Deber C. M. α-helical, but not β-sheet propensity of proline is determined by peptide environment. Proc. Natl. Acad. Sci. USA. 93:1996;6676-6681.
25. MacArthur M. W., Thornton J. M. Influence of proline residues on protein conformation. J. Mol. Biol. 218:1991;397-412.
26. Nilges M., Clore G. M., Gronnenborn A. M. Determination of three-dimensional structure of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett. 229:1988;317-324.
27. Poumbourios P., Ahmar W., McPhee D. A., Kemp B. E. Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure. J. Virol. 69:1995;1209-1218.
28. Tan K., Liu J., Wang J., Shen S., Lu M. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA. 94:1997;12303-12308.
29. von Heijne G. Proline kinks in transmembrane α-helices. J. Mol. Biol. 218:1991;499-503.
30. Weissenhorn W., Dessen A., Harrison S. C., Skehel J. J., Wiley D. C. Atomic structure of the ectodomain of HIV-1 gp41. Nature. 387:1997;426-430.
31. Wild C., Oas T., McDanal C., Bolognesi D., Matthews T. A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA. 89:1992;10537-10541.
32. Williams K. A., Deber C. M. Proline residues in transmembrane helices: Structural or dynamic role. Biochemistry. 30:1991;8219-8223.
33. Wishart D. S., Sykes B. D., Richards F. M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:1991;311-333.
34. Woolfson D. N., Williams D. H. The influence of proline residues on α-helical structure. FEBS Lett. 277:1990;185-188.
35. Wu C. S., Ikeda K., Yang J. T. Ordered conformation of polypeptide and proteins in acidic dodecyl sulfate solution. Biochemistry. 20:1981;566-570.
36. Yun R. H., Anderson A., Hermans J. Proline in α-helix: Stability and conformation studies by dynamics simulation. Protein Struct. Funct. Genet. 10:1991;219-228.
37. Zimm B. H. The scattering of light and the radial distribution function of high polymer solutions. J. Chem. Phys. 16:1948;1093-1099.