1H NMR assignments of apo calcyclin and comparative structural analysis with calbindin d(9k) and s 100β

Protein Science

Volumn 5, Issue 11, 1996, Pages 2162-2174

  Potts, Barbara C M ^c   Carlström, Göran ^a,c   Okazaki, Katsuo ^b,c   Hidaka, Hiroyoshi ^b,c   Chazin, Walter J ^c  

^a LUND UNIVERSITY   (Sweden)

^b NAGOYA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

calcyclin; chemical shift; EF hand calcium binding protein; homology; hydrophobic core; S100 protein

Indexed keywords

CALBINDIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; PROTEIN S 100; CALCIUM BINDING PROTEIN; PROTON;

ARTICLE; CALCULATION; CELL CYCLE G1 PHASE; GENE EXPRESSION; HYDROGEN BOND; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; AMINO ACID SEQUENCE; CHEMISTRY; COMPARATIVE STUDY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

AMINO ACID SEQUENCE; CALCIUM-BINDING PROTEIN, VITAMIN D-DEPENDENT; CALCIUM-BINDING PROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTONS; S100 PROTEINS;

EID: 0029658223     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560051103     Document Type: Article

References (88)

1. Aho AV, Kernighan BW, Weinberger PJ. 1988. The AWK programming language. Reading, Massachusetts: Addison-Wesley.
2. 9k determined by nuclear magnetic resonance spectroscopy. Biochemistry 31:1011-1020.
3. I,II binding pathway J Mol Biol 252:102-121.
4. 15N NMR assignments and solution secondary structure of rat Apo-S100ß. J Biomol NMR 6:171-179.
5. Barger SW, Wolchok SR, van Eldik LJ. 1992 Disulfide-linked S100β dimers and signal transduction. Biochim Biophys Acta 1160:105-112.
6. 1H nuclear magnetic resonance spectra. J Mol Biol 155:321-346.
7. Borgias BA, James TL. 1990. MARDIGRAS - A procedure for matrix analysis of relaxation for discerning geometry of an aqueous structure. J Magn Reson 87:475-487.
8. Braunschweiler L, Bodenhausen G, Ernst RR. 1983. Analysis of networks of coupled spins by multiple quantum NMR. Mol Phys 48:535-560.
9. 1H NMR spectroscopy. Biochemistry 25:9826-9833.
10. Calabretta B, Kaczmarek L, Mars W, Ochoa D, Gibson CW, Hirschhorn RR, Baserga R. 1985. Cell-cycle-specific genes differentially expressed in human leukemias. Proc Natl Acad Sci USA 82:4463-4467.
11. 1-specific genes in human malignant myeloid cells. Proc Natl Acad Sci USA 83:1495-1498.
12. 1H NMR spectra of proteins as probes of surface structure and dynamics FEBS Lett 222:109-114.
13. 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Application of an integrated approach to spin system identification in proteins. J Mol Biol 202:603-622
14. 1H spin systems in proteins. Biopolymers 26:973-977.
15. 2O solution. J Magn Reson 72:358-363
16. Crivici A, Ikura M. 1995. Molecular and structural basis of target recognition by calmodulin. Annu Rev Biophys Biomol Struct 24:86-116.
17. Davis DG. 1989. Elimination of baseline distortions and minimization of artifacts from phased 2D NMR spectra. J Magn Reson 81:603-607.
18. Dell'Angelica EC, Schleicher CH, Santome JA. 1994. Primary structure and binding properties of calgranulin C, a novel S100-like calcium-binding protein from pig granulocytes. J Biol Chem 269:28929-28936.
19. Delsuc MA, Lallemand JY. 1986. Improvement of dynamic range in NMR by oversampling. J Magn Reson 69:504-507.
20. Eisenberg D. 1984. Three-dimensional structure of membrane and surface proteins. Annu Rev Biochem 55:595-623.
21. Findlay WA, Sonnichsen FD, Sykes BD 1994. Solution structure of the TR1C fragment of skeletal muscle troponin-C. J Biol Chem 269:6773-6778.
22. Finn BE, Evenas J, Drakenberg T, Waltho JP, Thulin E, Forsén S. 1995. Calcium-induced structural changes and domain autonomy in calmodulin. Nature Struct Biol 2:777-783.
23. Gerke V, Weber K. 1985. Calcium-dependent conformational changes in the 36-kDa subumt of intestinal protein I related to the cellular 36-kDa target of rous sarcoma virus tyrosine kinase. J Biol Chem 260:1688-1695.
24. Güntert P, Braun W, Wuthrich K. 1991. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOSMA. J Mol Biol 277:517-530.
25. Güntert P, Wüthrich K 1991 Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J Biomol NMR 1:447-456.
26. Guo X, Chambers AF, Parfett CLJ, Waterhouse P, Murphy LC, Reid RE, Craig AM, Edwards DR, Denhardt DT. 1990. Identification of a serum-inducible messenger RNA (5B10) as the mouse homologue of calcyclin: Tissue distribution and expression m metastatic, ras-transformed NIH 3T3 cells. Cell Growth Diff 1:333-338.
27. Harper ET, Rose GD. 1993. Helix stop signals in proteins and peptides: The capping box. Biochemistry 32:7605-7609.
28. 1H proximities in solution Bull Math Biol 46:673-698
29. Hilt DC, Kligman D. 1991. The S-100 protein family: A biochemical and functional overview New York: Springer-Verlag.
30. Hirschhorn RR, Aller P, Yuan Z, Gibson CW, Baserga R. 1984. Cell-cycle-specific cDNAs from mammalian cells temperature sensitive for growth. Proc Nad Acad Sci USA 81:6004-6008.
31. 2+-binding site of troponin C by nuclear magnetic resonance spectroscopy. Biochemistry 30:4323-4333.
32. Keepers JW, James TL. 1984 A theoretical study of distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra. J Magn Reson 57:404-426.
33. Kilby PM, van Eldik LJ, Roberts GCK. 1995. Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein. FEBS Lett 363:90-96.
34. Kim Y, Prestegard JH. 1989. Measurement of vicinal couplings from cross peaks in COSY spectra. J Magn Reson 84:9-13.
35. Kligman D, Hilt DC. 1988. The S100 protein family. Trends Biochem Sci 13:437-443.
36. Kline AD, Braun W, Wüthrich K. 1988. Determination of the complete three-dimensional structure of the α-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry. J Mol Biol 204:615-724.
37. 9k. J Mol Biol 231 711-734.
38. Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
39. Krebs J, Quadroni M, van Eldik LJ. 1995. Dance of the dimers. Nature Struct Biol 2:711-714.
40. Kube E, Becker T, Weber K, Gerke V. 1992. Protein-protein interaction studied by site-directed mutagenesis. J Biol Chem 267:14175-14182.
41. Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. 1995. Solution structure of calcium-free calmodulin. Nature Struct Biol 2:768-776.
42. Kumar A, Ernst RR, Wuthrich K. 1980. A two-dimensional nuclear overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem Biophys Res Commun 95:1-6.
43. Kuznicki J, Filipek A, Hunziker PE, Huber S, Heizmann CW 1989. Calcium-binding protein from mouse Ehrlich ascites-tumor cells is homologous to human calcyclin. Biochem J 263:951-956.
44. Ludvigsen S, Poulsen FM. 1992. Positive φ-angles in proteins by nuclear magnetic resonance spectroscopy. J Biomol NMR 2:227-233.
45. Lyu PC, Wemmer DE, Zhou HX, Pinker RJ, Kallenbach NR. 1993. Capping interactions in isolated α-helices: Position-dependent substitution effects and structure of a serine-capped peptide helix. Biochemistry 32:421-425.
46. Macura S, Ernst RR. 1980. Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. Mol Phys 41:95-117.
47. 1H spin-spin coupling constants in proteins. Biochem Biophys Res Commun 113:967-974.
48. 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J Biomol NMR 5:14-24.
49. Minami H, Tokumitsu H, Mizutani A, Watanabe Y, Watanabe M, Hidaka H. 1992. Specific binding of CAP-50 to calcyclin. FEBS Lett 305:217-219.
50. 2, ridges in 2D NMR spectra and procedures for suppression. J Magn Reson 66:187-193
51. Pearlman DA, Case DA, Caldwell JC, Seibel GL, Singh UC, Weiner P, Kollman PA. 1991a. SANDER/AMBER 4.0 San Francisco, California: University of California.
52. Pearlman DA, Case DA, Yip P. 1991b. SANDER/AMBER 4.0. San Francisco, California: University of California,
53. Pedrocchi M, Schafer BW, Durussel I, Cox JA, Heizmann CW. 1994. Purification and characterization of the recombinant human calcium-binding S100 protein CAPL and CACY. Biochemistry 33:6732-6738.
54. Plateau P, Guéron M. 1982. Exchangeable proton NMR without base-line distortion, using new strong-pulse sequences. J Am Chem Soc 104:7310-7311.
55. 2+-binding proteins. Nature Struct Biol 2:790-796.
56. Rance M. 1987. Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J Magn Reson 74:557-564.
57. Ranee M, Byrd RA. 1983. Obtaining high-fidelity spin-1/2 powder spectra in anisotropic media: Phase-cycled Hahn echo spectroscopy. J Magn Reson 52:221-240.
58. 1H NMR spectra of proteins via double quantum filtering. Biochem Biophys Res Commun 117:479-485.
59. Shaka AJ, Lee CJ, Pines A. 1988. Iterative schemes for bilinear operators; applications to spin decoupling. J Magn Reson 77:274-293
60. Shaw GS, Hodges RS, Sykes BD. 1992. Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy. Biochemistry 31:9572-9580.
61. 9k. Biochemistry 29:5752-5761.
62. 9k. J Mol Biol 227:1100-1117.
63. Skelton NJ, Kördel J, Akke M, Forsén S, Chazin WJ. 1994. Signal transduction versus buffering activity in Ca2+-binding proteins. Nature Struct Biol 1:239-245.
64. 9k by NMR spectroscopy. J Mol Biol 249:441-462.
65. Smith SP, Barber KR, Dunn SD, Shaw GS. 1996. Structural influence of cation binding to recombinant human brain S100b. Evidence for calcium-induced exposure of a hydrophobic surface. Biochemistry 35:8805-8814.
66. Strynadka NCJ, James MNG. 1989. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu Rev Biochem 58:951-998.
67. 9k observed by X-ray crystallography. J Mol Biol 223:601-606.
68. Szebenyi DME, Moffat K. 1986. The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. J Biol Chem 261:8761-8777.
69. Teigelkamp S, Bhardwaj RS, Roth J, Meinardus-Hager G, Karas M, Sorg C. 1991. Calcium-dependent complex assembly of the myeloic differentiation proteins MRP-8 and MRP-14. J Biol Chem 266:13462-13467.
70. Tokumitsu H, Kobayashi R, Hidaka H 1991. A calcium-binding protein from rabbit lung cytosol identified as the product of growth-regulated gene (2A9) and its binding proteins. Arch Biochem Biophys 288:202-207.
71. 2-terminal domain of rabbit CAP-50 (annexin XI): Functional expression of CAP-50 in Eschericha coli. Arch Biochem Biophys 303:302-306.
72. 2+/phospholipid-binding proteins, annexin family. J Biol Chem 267:8919-8924.
73. Tropp J. 1980. Dipolar relaxation and nuclear Overhauser effects in nonrigid molecules: The effect of fluctuating internuclear distances. J Chem Phys 72:6035-6043.
74. Wagner G. 1983. Two-dimensional relayed coherence transfer spectroscopy of a protein. J Magn Reson 55:151-156.
75. Watanabe M, Ando Y, Tokumitsu H, Hidaka H. 1993. Binding site of annexin XI on the calcyclin molecule. Biochem Biophys Res Commun 196:1376-1382
76. Weber C, Lee VD, Chazin WJ, Huang B. 1994. High level expression in Escherichia coli and characterization of the EF-hand calcium-binding protein caltractin. J Biol Chem 269 15795-15802.
77. Weterman MAJ, Stoopen GM, Muijen GNPv, Kuznicki J, Ruiter DJ, Bloemers HPJ. 1992 Expression of calcyclin in human melanoma cell lines correlates with metastatic behavior m nude mice. Cancer Res 52:1291-1296.
78. Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD 1995. H-1, C-13 and N-15 chemical shift referencing in biomolecular NMR. J Biomol NMR 6 135-140.
79. Wishart DS, Sykes BD, Richards FM. 1991 Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333.
80. Wishart DS, Sykes BD, Richards FM. 1992. The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651.
81. Wojda U, Kuznicki J. 1994. Calcyclin from mouse Ehrlich ascites tumor cells and rabbit lung form non-covalent dimers. Biochim Biophys Acta 1209:248-252.
82. Wüthrich K. 1986. NMR of proteins and nucleic acids. New York: John Wiley & Sons.
83. Wüthrich K, Billeter M, Braun W. 1983. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J Mol Biol 169:949-961.
84. Wüthrich K, Billeter M, Braun W. 1984 Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J Mol Biol 180 715-740.
85. Yip PF. 1990. Scaling NOESY cross peaks involving methyl protons. J Magn Reson 90:382-383.
86. Zeng F, Gabius H. 1991 Carbohydrate-binding specificity of calcyclin and its expression in human tissues and leukemic cells. Arch Biochem Biophys 289:137-144.
87. Zeng F, Gerke V, Gabius H. 1993. Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart. Int J Biochem 25:1019-1027.
88. Zhang M, Tanaka T, Ikura M. 1995. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct Biol 2:758-767.