Solution structure of the coiled-coil trimerization domain from lung surfactant protein D

Journal of Biomolecular NMR

Volumn 24, Issue 2, 2002, Pages 89-102

  Kovacs, Helena ^c,d   O'Donoghue, Sean I ^c,e   Hoppe, Hans Jürgen ^b   Comfort, David ^a,g   Reid, Kenneth B M ^b   Cambell, Ian D ^a   Nilges, Michael ^c,f  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^d BRUKER BIOSPIN AG   (Switzerland)

^e Axaron Bioscience AG   (Germany)

^f INSTITUT PASTEUR   (France)

^g UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Ambiguous distance restraints; Coiled coil; Lung surfactant protein; NMR spectroscopy; Trimer

Indexed keywords

LEUCINE ZIPPER PROTEIN; LUNG SURFACTANT; PEPTIDE; SURFACTANT PROTEIN D; TETRAMER; TYROSINE;

ALLERGIC REACTION; AMINO ACID ANALYSIS; ANALYTIC METHOD; ANTIGENICITY; CALCULATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; IMMUNE RESPONSE; LUNG ALVEOLUS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERIZATION; POLYMERIZATION; PREDICTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; TRIPLE HELIX; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SOLUTION AND SOLUBILITY;

AMINO ACID SEQUENCE; HUMANS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PULMONARY SURFACTANT-ASSOCIATED PROTEIN D; PULMONARY SURFACTANTS; REPETITIVE SEQUENCES, AMINO ACID; SOLUTIONS;

EID: 0242303422     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020980006628     Document Type: Review

References (53)

1. Bartels, C., Xia, T., Billeter, M., Güntert, P. and Wüthrich, K. (1995) J. Biomol. NMR, 5, 1-10.
2. Betz, S.F., Bryson, J.W. and DeGrado, W.F (1995) Curr. Opin. Struct. Biol., 5, 457-463.
3. Brünger, A.T. (1993) X-Plor Version 3.1, Yale University Press, New Haven, U.S.A.
4. Caffrey, M., Cai, M., Kaufman, J., Stahl, S.J., Wingfield, PT., Gronenborn, A.M. and Clore, G.M. (1997) J. Mol. Biol., 271, 819-826.
5. Chan, D.C., Fass, D., Berger, J.M. and Kim, P.S. (1997) Cell, 89, 263-273.
6. Clore, G.M., Omichinski, J.G., Sakaguchi, K., Zambrano, N., Appella, E. and Gronenborn, A. (1995) Science, 267, 1515-1516.
7. Crick, F.H.C. (1953) Acta Crystallogr., 6,589-697.
8. Dames, S.A., Kammerer, R.A., Wiltscheck, R., Engel, J. and Alexandrescu, A.T. (1998) Nat. Struct. Biol., 5, 687-691.
9. Fass, D., Harrison, S.C. and Kim, P.S. (1996) Nat. Struct. Biol., 3, 465-469.
10. Folmer, R.H.A., Hilbers, C.W., Konings, R.N.H. and Nilges, M. (1997) J. Biomol. NMR, 9, 245-258.
11. Gonzalez, L., Plecs, J.J. and Alber, T. (1996a) Nat. Struct. Biol., 3, 510-515.
12. Gonzalez, L., Brown, R.A., Richardson, D. and Alber, T. (1996b) Nature Struct. Biol., 3, 1002-1009.
13. Gordon-Smith D.J., Carbajo R.J., Yang J.C., Videler H., Runswick M.J., Walker J.E. and Neuhaus D. (2001). J. Mol. Biol., 308, 325-339.
14. Güntert, P., Mumenthaler, C. and Wüthrich, K. (1997) J. Mol. Biol., 273, 283-298.
15. Hakansson, K., Lim, N.K., Hoppe, H.-J. and Reid, K.B.M. (1999) Structure, 7, 1-10.
16. Harbury, P.B., Kim, P.S. and Alber, T. (1994) Nature, 371, 80-83.
17. Harbury, P.B., Zhang, T., Kim, P.S. and Alber, T. (1993) Science, 262, 1401-1407.
18. Hidalgo P., Ansari A.Z., Schmidt P., Hare B., Simkovich N., Farrell S., Shin E.J., Ptashne M. and Wagner G. (2001) Genes. Dev., 15, 1007-1020.
19. Holmskov, U., Malhotra, R., Sim, R.B. and Jensenius, J.C. (1994) Immunol. Today, 15, 67-73.
20. Hoppe, H.-J. and Reid, K.B.M. (1994) Prot. Sci., 3, 1143-1158.
21. Hoppe, H.A., Barlow, P.N. and Reid, K.B.M. (1994) FEBS Lett., 344, 191-195.
22. Jasanoff, A. (1998). J. Biomol. NMR, 12, 299-306.
23. Johansson, J., Curstedt, T. and Robertson, B. (1994) Eur. Respir. J., 7, 372-391.
24. Junius, F.K., O'Donoghue S.I., Nilges, M., Weiss, A.S. and King, G.F. (1996) J. Biol. Chem., 271, 13663-13667.
25. King, G.F. (1996) Biophys. J., 71, 1-2.
26. Kishore, U., Wang, J.-Y., Hoppe, H.-J. and Reid, K.B.M. (1996) Biochem. J., 318, 505-511.
27. Koradi, R., Billeter, M. and Wüthrich, K. (1996) J. Mol. Graphics, 14, 51-55.
28. Kraulis, P.J. (1991) J. Appl. Crystallogr., 24, 946-950.
29. Landschultz, W.H., Johnson, P.F. and McKnight, S.L. (1988) Science, 240, 1759-1764,
30. Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Moss, D.S., Kaptein, R. and Thornton, J.M. (1993) J. Biomol. NMR, 8, 477-486.
31. Linge, J.P. and Nilges, M. (1999) J. Biomol. NMR, 13, 51-59.
32. Lovejoy, B., Choe, S., Cascio, D., McRorie, D.K., DeGrado, W.F. and Eisenberg, D. (1993) Science, 259, 1288-1293.
33. MacKay, J.P., Shaw, G.L. and King, G.F. (1996) Biochemistry, 35, 4867-4877.
34. Miyamura, K., Leigh, L.E.A., Hopkin, J., Lopez-Bernal, A. and Reid, K.B.M. (1994) Biochem. J., 300, 237-242.
35. Nicholls, A. and Honig, B. (1991) J. Comput. Chem., 12, 435-445.
36. Nilges, M. (1993) Proteins, 17, 297-309.
37. Nilges, M. and Brünger, A.T. (1991) Protein Eng., 4, 649-659.
38. Nilges, M. and O'Donoghue, S.I. (1998) Progr NMR Spectrosc., 32, 107-139.
39. Nilges, M., Clore, G.M. and Gronenborn, A.M. (1988a) FEBS Lett., 229, 317-324.
40. Nilges, M., Gronenborn, A.M., Brünger, A.T. and Clore, G.M. (1988b) Protein Eng., 2, 27-38.
41. Nilges, M., Macias, M., O'Donoghue S.I. and Oschkinat, H. (1997) J. Mol. Biol., 269, 408-422.
42. Nooren, I.M., Kaptein R., Sauer R.T. and Boelens R. (1999) Nature Struct. Biol., 6, 755-759.
43. O'Donoghue, S.I. and Nilges, M. (1999) In Biological Magnetic Resonance, Vol. 17, Berliner, J.L. and Krishna, N.R. (Eds.), Plenum, New York pp. 131-161.
44. O'Donoghue, S.I., Chang, X., Abseher, R., Nilges, M. and Led, J.J. (2000) J. Biomol. NMR, 16, 93-108.
45. O'Donoghue, S.I., Junius, F.K. and King, G.F. (1993) Protein Eng., 6, 557-564.
46. O'Donoghue, S.I., King, G.F. and Nilges, M (1996) J. Biomol. NMR, 8, 193-206.
47. Ogihara, N.L., Weiss, M.S., Degrado, W.F. and Eisenberg, D. (1997) Protein Sci., 6, 80-88.
48. Pascual, J., Pfuhl, M., Walther, D., Saraste, M. and Nilges, M. (1997) J. Mol. Biol., 273, 740-751.
49. Sheriff, S. , Chang, C.Y. and Ezekowitz, R.A.B. (1994) Nat. Struct. Biol., 1, 789-794.
50. Thiel, S. and Reid, K.B.M. (1989) FEBS Lett., 250, 78-84.
51. Weaver, T.E. and Whitsett, J.A. (1991) Biochem. J. 273, 249-264.
52. Weis, W.I. and Drickamer, K. (1994) Structure, 2, 1227-1240.
53. Wilson, I.A., Skehel, J.J. and Wiley, D.C. (1981) Nature 289, 366-373.