Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein

Protein Science

Volumn 14, Issue 7, 2005, Pages 1894-1901

  Venkitaramani, Deepa V ^a   Fulton, D Bruce ^a   Andreotti, Amy H ^a   Johansen, Kristen M ^a   Johansen, Jørgen ^a  

^a IOWA STATE UNIVERSITY   (United States)

Author keywords

Calcium binding proteins; Calsensin; Dynamics; EF hand; Helix loop helix; Nervous system; NMR structure

Indexed keywords

BINDING PROTEIN; NITROGEN;

ARTICLE; CALCIUM BINDING; CONFORMATION; MEASUREMENT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN SYNTHESIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM-BINDING PROTEINS; EF HAND MOTIFS; LEECHES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; NEURONS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS; THERMODYNAMICS;

HIRUDINIDA; INVERTEBRATA;

EID: 22244474963     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051412605     Document Type: Article

References (60)

1. 2+. Protein Sci. 10: 74-82.
2. Andersson, P., Gsell, B., Wipf, B., Senn, H., and Otting, G. 1998. HMQC and HSQC experiments with water flip-back optimized for large proteins. J. Biomol. NMR 11: 279-288.
3. Berridge, M.J., Bootman, M.D., and Lipp, P. 1998. Calcium - A life and death signal. Nature 395: 645-648.
4. 2+/S100B/NDR kinase peptide complex: Insights into S100 target specificity and activation of the kinase. Biochemistry 42: 14416-14426.
5. 2+ coordination. Biochemistry 37: 7617-7629.
6. Brazin, K.N., Fulton, D.B., and Andreotti, A.M. 2000. A specific intermolecular association between the regulatory domains of a Tec family kinase. J. Mol. Biol. 302: 607-623.
7. Briggs, K.K., Johansen, K.M., and Johansen, J. 1993. Selective pathway choice of a single central axonal fascicle by a subset of peripheral neurons during leech development. Dev. Biol. 158: 380-389.
8. Briggs, K.K., Silvers, A.J., Johansen, K.M., and Johansen, J. 1995. Calsensin: A novel calcium-binding protein expressed in a subset of peripheral leech neurons fasciculating in a single axon tract. J. Cell Biol. 129: 1355-1362.
9. Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., et al. 1998. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54: 905-921.
10. Cavanagh, J., Fairbrother, W.J., Palmer III, A.G., and Skelton, N.J. 1995. Protein NMR spectroscopy: Principles and practical approach. Academic Press, San Diego.
11. Cornilescu, G., Delaglio, F., and Bax, A. 1999. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13: 289-302.
12. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
13. Donato, R. 2001. S100: A multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell Biol. 33: 637-668.
14. _. 2003. Intracellular and extracellular roles of S100 proteins. Microsc. Res. Tech. 60: 540-551.
15. Dosset, P., Hus, J.C., Blackledge, M., and Marion, D. 2000. Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J. Biomol. NMR 16: 23-38.
16. Drohat, A.C., Baldisseri, D.M., Rustandi, R.R., and Weber, D.J. 1998. Solution structure of calcium-bound rat S100B (ββ) as determined by nuclear magnetic resonance spectroscopy. Biochemistry 37: 2729-2740.
17. Drohat, A.C., Tjandra, N., Baldisseri, D.M., and Weber, D.J. 1999. The use of dipolar couplings for determining the solution structure of rat apo-S100B (ββ). Protein Sci. 8: 800-809.
18. 15N NMR relaxation. Biochemistry 33: 5984-6003.
19. Fulton, D.B., Hrabal, R., and Ni, F. 1996. Gradient-enhanced TOCSY experiments with improved sensitivity and solvent suppression. J. Biomol. NMR 8: 213-218.
20. Griffin, S.W.T., Sheng, J.G., Royston, M.C., Gentleman, S.M., McKenzie, J.E., Graham, D.I., Roberts, G.W., and Mrak, R.E. 1998. Glial-neuronal interactions in Alzheimer's disease: The potential role of a "cytokine cycle" in disease progression. Brain Pathol. 8: 65-72.
21. 15N nuclear magnetic resonance relaxation studies on rat β-parvalbumin and the pentacarboxylate variants, S55D and G98D. Protein Sci. 11: 158-173.
22. Hong, K., Nishiyama, M., Henley, J., Tessier-Lavigne, M., and Poo, M. 2000. Calcium signalling in the guidance of nerve growth by netrin-1. Nature 403: 93-98.
23. Ikura, M. 1996. Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21: 14-17.
24. Ikura, M., Clore, G.M., Groneborn, A.M., Zhu, G., Klee, C.B., and Bax, A. 1992. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256: 632-638.
25. 15N NMR relaxation. Biochemistry 40: 3439-3445.
26. Johnson, B.A. and Blevins, R.A. 1994. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4: 603-614.
27. 2O samples of proteins. J. Magn. Reson. B 101: 333-337.
28. 9k: A protein optimized for calcium-binding at neutral pH. Biochemistry 40: 15334-15340.
29. Koradi, R., Billeter, M., and Wuthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-55.
30. Kuboniwa, H., Grzesiek, S., Delaglio, F., and Bax, A. 1994. Measurement of HN-H α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4: 871-878.
31. Lippens, G., Dhalluin, C., and Wieruszeski, J.-M. 1995. Use of water flip-back pulse in the homonuclear NOESY experiment. J. Biomol. NMR5: 327-331.
32. Maler, L., Potts, B.C.M., and Chazin, W.J. 1999. High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins. J. Biomol. NMR 13: 233-247.
33. 2+-Calcyclin. J. Mol. Biol. 317: 270-290.
34. 9k. Biochemistry 37: 2586-2595.
35. Malmendal, A., Evenas, J., Forsen, S., and Akke, M. 1999. Structural dynamics in the C-terminal domain of Calmodulin at low calcium levels. J. Mol. Biol. 293: 883-899.
36. Mandel, A.M., Akke, M., and Palmer III, A.G. 1995. Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme. J. Mol. Biol. 246: 144-163.
37. Markley, J.L., Bax, A., Arata, Y., Hilbers, C.W., Kaptien, R., Sykes, B.D., Wright, P.E.,and Wuthrich, K. 1998. Recommendations for the presentation of NMR structures of proteins and nucleic acids. J.Mol. Biol. 280: 933-952.
38. Mori, S., Abeygunawardana, C., O'Neil Johnson, M., and van Zijl, P.C.M. 1995. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Magn. Reson. B 108: 94-98.
39. Muhandiram, D.R., and Kay, L.E. 1994. Gradient enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. B 103: 203-216.
40. 2O. J. Magn. Reson. B 102: 317-321.
41. 2+ binding. Biometals 11: 297-318.
42. 2+ sensor proteins. Protein Sci. 7: 270-282.
43. Neudecker, P., Nerkamp, J., Eisenmann, A., Nourse, A., Lauber, T., Schweimer, K., Lehmann, K., Schwarzinger, S., Ferreira, F., and Rosch, P. 2004. Solution structure, dynamics and hydrodynamics of the calcium-bound cross-reactive birch pollen allergen Bet v 4 reveal a canonical monomeric two EF-hand assembly with a regulatory function. J. Mol. Biol. 336: 1141-1157.
44. Niederberger, V., Hayek, B., Vrtala, S., Laffer, S., Twardosz, A., Vangelista, L., Sperr, W.R., Valent, P., Rumpold, H., Kraft, D., et al. 1999. Calcium-dependent immunoglobulin E recognition of the apo- and calcium-bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. FASEB J. 13: 843-856.
45. Piantini, U., Sorensen, O.W., and Ernst, R.R. 1982. Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104: 6800-6801.
46. 9k and S100β. Protein Sci. 5: 2162-2174.
47. Roberts, G.C.K. 1993. NMR of macromolecules: A practical approach. Oxford University Press, Oxford, UK.
48. Schafer, B.W. and Heizmann, C.W. 1996. The S100 family of EF-hand calcium-binding proteins: Functions and pathology. Trends Biochem. Sci. 21: 134-140.
49. Smith, S.P., Barber, K.R., Dunn, S.D., and Shaw, G.S. 1996. Structural influence of cation binding to recombinant human brain S100b: Evidence for calcium-induced exposure of a hydrophobic surface. Biochemistry 35: 8805-8814.
50. Talluri, S. and Wagner, G. 1996. An optimized 3D NOESY-HSQC. J. Magn. Reson. B 112: 200-205.
51. 15N relaxation at four fields, reveals unique mobility characteristics of the intermotif linker. Protein Sci. 10: 1393-1402.
52. Theret, I., Baladi, S., Cox, J.A., Gallay, J., Sakamoto, H., and Craescu, C.T. 2001b. Solution structure and backbone dynamics of the defunct domain of calcium vector protein. Biochemistry 40: 13888-13897.
53. 15N NMR relaxation. J. Am. Chem. Soc. 117: 12562-12566.
54. Vallely, K.M., Rustandi, R.R., Ellis, K.C., Varlamova, O., Bresnick, A.R., and Weber, D.J. 2002. Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy. Biochemistry 41: 12670-12680.
55. 2+-calmodulin signaling in Drosophila growth cones leads to stalls in axon extension and errors in axon guidance. Neuron 14: 43-56.
56. Verdina, P., Westritschnig, K., Valenta, R., and Keller, W. 2002. The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly. EMBO J. 21: 5007-5016.
57. Wuthrich, K. 1986. NMR of proteins and nucleic acids. Wiley, New York.
58. Yap, K.L., Ames, J.B., Swindells, M.B., and Ikura, M. 1999. Diversity of conformational states and changes within the EF-hand protein superfamily. Proteins 37: 499-507.
59. Zheng, J.Q. 2000. Turning of nerve growth cones induced by the localized increases in intracellular calcium ions. Nature 403: 89-93.
60. Zimmer, D.B., Cornwall, E.H., Landar, A., and Song, W. 1995. The S100 protein family: History, function, and expression. Brain Res. Bull. 37: 417-429.