A calbindin D(9k) mutant containing a novel structural extension: 1H nuclear magnetic resonance studies

Protein Science

Volumn 6, Issue 2, 1997, Pages 323-330

  Groves, Patrick ^a,b   Linse, Sara ^a   Thulin, Eva ^a   Forsén, Sture ^a  

^a LUND UNIVERSITY   (Sweden)

^b NENCKI INSTITUTE OF EXPERIMENTAL BIOLOGY   (Poland)

Author keywords

calbindin D(9k); calcium binding constants; calcium binding protein; induced structure; NMR assignment

Indexed keywords

CALBINDIN; HELIX LOOP HELIX PROTEIN; PROTON;

ARTICLE; CALCIUM TRANSPORT; ENTROPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RECEPTOR AFFINITY; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION;

AMINO ACID SEQUENCE; CALCIUM-BINDING PROTEIN, VITAMIN D-DEPENDENT; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTONS;

EID: 0030614689     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060207     Document Type: Article

References (49)

1. 15N NMR relaxation. Biochemistry 32:9832-9844.
2. Babu YS, Bugg CE, Cook WJ. 1988. Structure of calmodulin refined at 2.2 Å resolution. J Mol Biol 204:191-204.
3. Bothner-By A, Stephens R, Lee J-M, Warren C, Jeanloz R. 1984. Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame. J Am Chem Soc 706:811-813.
4. Braunschweiler L, Bodenhausen G, Ernst R. 1983. Analysis of networks of coupled spins by multiple quantum NMR. Mol Phy 48:535-560.
5. Braunschweiler L, Ernst R. 1983. Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J Magn Reson 53:521-528.
6. Brodin P, Grundström T, Hofmann T, Drakenberg T, Thulin E, Forsén S. 1986. Expression of bovine intestinal CaBP from a synthetic gene in Escherichia coli and characterization of the product. Biochemistry 25:5371-5377.
7. 2+ binding. J Mol Biol 231:415-430.
8. 1H NMR. Biochemistry 28:8646-8653.
9. 28k synthesised in bacteria. Eur J Biochem 215:401-410.
10. Cook WJ, Jeffrey LC, Cox JA, Vijay-Kumar S. 1993. Structure of a sarcoplasmic calcium-binding protein from amphioxus refined at 2.4 Å resolution. J Mol Biol 229:461-471.
11. Drohat AC, Amburgey JC, Abildgaard F, Starlich MR, Baldisseri D, Weber DJ. 1996. Solution structure of rat apo-S100B (ββ) as determined by NMR spectroscopy. Biochemistry 35:11577-11588.
12. Finn BE, Evenäs 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.
13. Flaherty KM, Zozulya S, Stryer L, McKay DB. 1993. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell 75:709-716.
14. Fullmer C, Wasserman R. 1987. Chicken intestinal 28-kilodalton calbindin-D: Complete amino acid sequence and structural considerations. Proc Natl Acad Sci USA 84:4772-4776.
15. Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. 1992. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256:632-638.
16. Ikura M. 1996. Calcium binding and conformational response in EF-hand proteins. TIBS 21:14-17.
17. Isobe T, Okuyama T. 1978. The amino acid sequence of S-100 protein (PAP I-b protein) and its relation to the calcium-binding proteins. Eur J Biochem 89:379-388.
18. 9k. Biochemistry 28:7065-7074.
19. 9k: NMR studies of the minor (cis-Pro 43) isoform and the Pro 43 Gly mutant. Biochemistry 29:4400-4409.
20. 9k. J Mol Biol 231:711-734.
21. 15N NMR spectroscopy. Biochemistry 31:4856-4866.
22. Kretsinger R, Nockolds C. 1973. Carp muscle calcium-binding protein: Structure determination and general description. J Biol Chem 248:3313-3326.
23. 9k. Biochemistry 26:6723-6735.
24. Linse S, Brodin P, Johansson C, Thulin E, Grundström T, Forsén S. 1988. The role of protein surface charges in ion binding. Nature 335:651-652.
25. 9k. Biochemistry 30:154-162.
26. 9k: Stability, calcium binding and NMR studies. Protein Sci 2:985-1000.
27. 1H spin-spin coupling constants in proteins. Biochem Biophys Res Commun 113:967-974.
28. Meador WE, Means AR, Quiocho FA. 1992. Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 257:1251-1255.
29. 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.
30. Mueller L. 1987. PECOSY, a simple alternative to ECOSY. J Magn Reson 72:191-196.
31. 1H-NMR techniques for the identification of the amino-acid-proton spin systems in proteins (Rabbit metallothionein-2). Eur J Biochem 151:257-273.
32. O'Neil K, DeGrado W. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250:646-651.
33. Schäfer BW, Heizmann CW. 1996. The S100 family of EF-hand calcium-binding proteins: Functions and pathology. TIBS 21:134-140.
34. 2 states. FEBS Letters 303:136-140.
35. 9k. J Mol Biol 213:593-598.
36. 9k determined by NMR spectroscopy. J Mol Biol 249:441-462.
37. States D, Haberkorn R, Ruben D. 1982. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J Magn Reson 48:286-292.
38. 9k observed by X-ray crystallography. J Mol Biol 223:601-606.
39. Swindells MB, Ikura M. 1996. Pre-formation of the semi-open conformation by the apo-calmodulin C-terminal domain and implications for binding IQ-motifs. Nature Struct Biol 2:501-504.
40. Szebenyi D, Moffat K. 1986. The refined structure of vitamin D-dependent CaBP from bovine intestine. J Biol Chem 267:8761-8777.
41. Tanaka T, Ames JB, Harvey TS, Stryer L, Ikura M. 1995. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376:444-441.
42. Vijay-Kumar S, Cook WJ. 1992. Structure of a sarcoplasmic calcium-binding protein from Nereisdiversicolor refined at 2.0 Å resolution. J Mol Biol 224:413-426.
43. Wagner G. 1983. Two-dimensional relayed coherence transfer spectroscopy of a protein. J Magn Reson 55:151-156.
44. Wimberly B, Thulin E, Chazin WJ. 1995. Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant. Protein Sci 4:1045-1055.
45. Wishart D, Bigam C, Holm A, Hodges R, Sykes B. 1995. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J Biomol NMR 5:67-81.
46. Wishart D, Sykes B, Richards F. 1991. Relationship between NMR chemical shift and protein structure. J Mol Biol 222:311-333.
47. Wüthrich K, Billeter M, Braun W. 1984. Pseudostructures 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.
48. Wüthrich K. 1986. NMR of proteins and nucleic acids. John Wiley & Sons, New York.
49. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4:845-858.