Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy

Protein Science

Volumn 7, Issue 11, 1998, Pages 2421-2430

  Qian, Hong ^a   Rogers, Michael S ^b   Schleucher, Jürgen ^a   Edlund, Ulf ^a   Strehler, Emanuel E ^b   Sethson, Ingmar ^a  

^a UMEÅ UNIVERSITY   (Sweden)

^b MAYO GRADUATE SCHOOL   (United States)

Author keywords

Calmodulin like protein; NMR; Secondary structural analysis; Sequential assignment

Indexed keywords

CALMODULIN; CARBON 13; NITROGEN 15; PROTON; CALCIUM BINDING PROTEIN;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN POLYMORPHISM; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; AMINO ACID SEQUENCE; CHEMISTRY; COMPARATIVE STUDY; HUMAN; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; SEQUENCE ALIGNMENT;

VERTEBRATA;

AMINO ACID SEQUENCE; CALCIUM-BINDING PROTEINS; CALMODULIN; HUMANS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

EID: 0031593361     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071120     Document Type: Article

References (44)

1. Bax A, Pochapsky SS. 1992. Optimized recording off heteronuclear multidimensional NMR spectra using pulsed field gradients. J Magn Reson 99:638-643.
2. Cavanagh J, Rance M. 1992. Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J Magn Reson 96:670-678.
3. Chattopadhyaya R, Meador WE, Means AR, Quiocho FA. 1992. Calmodulin structure refined at 1.7 Å resolution. J Mol Biol 228:1177-1192.
4. Clore GM, Gronenborn AM. 1989. Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. CRC Crit Rev Biochem Mol Biol 24:479-564.
5. Cohen P, Klee CB. 1988. Calmodulin. In molecular aspects of cellular regulation. Amsterdam: Elsevier.
6. Davis TN, Thorner J. 1989. Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable. Proc Natl Acad Sci USA 86:7909-7913.
7. Durussel I, Rhyner JA, Strehler EE, Cox JA. 1993. Cation binding and conformation of human calmodulin-like protein. Biochemistry 32:6089-6094.
8. Edman CF, George SE, Means AR, Schulman H, Yaswen P. 1994. Selective activation and inhibition of calmodulin-dependent enzymes by a calmodulin-like protein found in human epithelial cells. Eur J Biochem 226:725-730.
9. Fesik SW, Zuiderweg ERP. 1988. Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra. J Magn Reson 78:588-593.
10. Finn BE, Forsen S. 1995. The evolving model of calmodulin structure, function and activation. Structure 3:7-11.
11. Frenkiel T, Bauer C, Carr MD, Birdsall B, Feeney J. 1990. HMQC-NOESY-HMQC, a three-dimensional NMR experiment which allows detection of nuclear Overhauser effects between protons with overlapping signals. J Magn Reson 90:420-425.
12. Geiser JR, VanTuinen D, Brockerhoff SE, Neff MM, Davis, TN. 1991. Can calmodulin function without binding calcium? Cell 65:949-959.
13. Grezsiek S, Bax A. 1992. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114:6291-6293.
14. Harris E, Yaswen P, Thorner J. 1995. Gain-of-function mutations in a human calmodulin-like protein identify residues critical for calmodulin action in yeast. Mol Gen Genet 247:137-147.
15. Hickie RA, Graham MJ, Buckmeier JA, Meyskens FL Jr. 1992. Comparison of calmodulin gene expression in human neonatal melanocytes and metastatic melanoma cell lines. J Invest Dermatol 99:764-773.
16. Ikura M. 1996. Calcium binding and conformational response in EF-hand proteins. TIBS 21:14-17.
17. Ikura M, Bax A, Clore GM, Gronenborn AM. 1990. Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J Am Chem Soc 112:9020-9022.
18. Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. 1992. Solution structure of the calmodulin-target peptide complex by multi-dimensional NMR. Science 256:632-638.
19. 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy. Biochemistry 30:9216-9228.
20. Koller M, Strehler EE. 1988. Characterization of an intronless human calmodulin-like pseudogene. FEBS Lett 239:121-128.
21. Marion D, Ikura M, Tschudin R, Bax A. 1989. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Reson 85:393-399.
22. Meador WE, Means AR. Quiocho FA. 1992. Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257:1251-1255.
23. Meador WE, Means AR, Quiocho FA. 1993. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262:1718-1721.
24. Muhandiram DR, Kay LE. 1994. Gradient-enhanced triple-resonance three dimensional NMR experiments with improved sensitivity. J Magn Reson Ser B 103:203-216.
25. Ohya Y, Anraku Y. 1992. Yeast calmodulin: Structural and functional elements essential for the cell cycle. Cell Calcium 13:445-455.
26. Palmer AG III, Cavanagh J, Byrd RA, Rance M. 1992. Sensitivity improvement in three-dimensional heteronuclear correlation NMR spectroscopy. J Magn Reson 96:416-424.
27. Patt SL. 1992. Single and multiple-frequency-shifted laminar pulses. J Magn Reson 96:94-102.
28. Rasmussen CD, Means AR. 1987. Calmodulin is involved in regulation of cell proliferation. EMBO J 6:3961-3968.
29. Rasmussen CD, Means AR. 1989. Calmodulin is required for cell-cycle progression during G1 and mitosis. EMBO J 8:73-82.
30. Rhyner JA, Koller M, Durussel-Gerber I, Cox JA, Strehler EE. 1992. Characterization of the human calmodulin-like protein expressed in Escherichia coli. Biochemistry 31:12826-12832.
31. Rogers MS, Strehler EE. 1996. Calmodulin. In: Celio MR, ed. Guidebook to the calcium-binding proteins. Oxford, UK: Oxford University Press. pp 34-40.
32. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning: A laboratory manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
33. Slupsky CM, Kay CM, Reinach FC, Smillie LB, Sykes BD. 1995a. The calcium-induced dimerization of troponin C: The mode of interaction and the use of trifluoroethanol as a denaturant of quaternary structure. Biochemistry 54:7365-7375.
34. Slupsky CM, Reinach FC, Smillie LB, Sykes BD. 1995b. Solution secondary structure of calcium-saturated troponin C monomer determined by multi-dimensional heteronuclear NMR spectroscopy. Protein Sci 4:1279-1290.
35. 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 113:5490-5492.
36. Takemoto D, Jilka K. 1983. Increased content of calmodulin in human leukemic cells. Leukemia Res 7:97-100.
37. Torok K, Whitaker M. 1994. Taking a long, hard look at calmodulin's warm embrace. BioEssays 16:221-224.
38. Wei JW, Hickie RA. 1981. Increased content of calmodulin in Morris hepatoma 5123 t.c. (h). Biochim Biophys Res Commun 256:1562-1568.
39. 13C chemical-shift data. J Biomol NMR 4:171-180.
40. Wittekind M, Mueller L. 1993. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J Magn Reson Ser B 101:201-205.
41. Wüthrich K. 1986. NMR of proteins and nucleic acids. New York: John Wiley and Sons.
42. Yaswen P, Smoll A, Hosoda J, Parry G, Stampfer MR. 1992. Protein product of a human intronless calmodulin-like gene shows tissue-specific expression and reduced abundance in transformed cells. Cell Growth Diff 3:335-345.
43. Yaswen P, Smoll A, Peehl DM, Trask DK, Sager R, Stampfer MR. 1990. Down-regulation of a calmodulin-related gene during transformation of human mammary epithelial cells. Proc Natl Acad Sci USA 87:7360-7364.
44. 13C′-edited NOESY-H(N)CO experiment. J Magn Reson Ser B 111:305-309.