Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy

Protein Science

Volumn 8, Issue 12, 1999, Pages 2630-2638

  Zangger, Klaus ^a   Öz, Gülin ^a   Otvos, James D ^b   Armitage, Ian M ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

2D NMR; 113Cd; Accordion HMQC; Mouse metallothionein 1; Nuclear magnetic resonance; Structure

Indexed keywords

CADMIUM; CYSTINE; METALLOTHIONEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; MOUSE; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

MAMMALIA;

EID: 0342614962     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.12.2630     Document Type: Article

References (32)

1. 7] metallothionein-2a in aqueous solution determined by nuclear magnetic resonance spectroscopy. J Mol Biol 201:637-657.
2. Aue WP, Bartholdi E, Ernst RR. 1976. Two-dimensional spectroscopy. Application to nuclear magnetic resonance. J Chem Phys 64:2229-2246.
3. Binz PA, Kägi JHR. 1999. Metallothionein: Molecular evolution and classification. In: Klaassen CD, ed. Metallothionein IV. Basel: Birkhäuser Verlag. pp 7-13.
4. Bodenhausen G, Ruben DJ. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69:185-188.
5. Braunschweiler L, Ernst RR. 1983. Coherence transfer by isotropic mixing. Application to proton correlation spectroscopy. J Magn Reson 53:521-528.
6. Brunger AT, Clore GM, Gronenborn AM, Karplus M. 1986. Three-dimensional structures of proteins by molecular dynamics with interproton distance Restraints: Application to crambin. Proc Natl Acad Sci USA 83:3801-8305.
7. Clore GM, Gronenborn AM, Nilges M, Ryan CA. 1987. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restraint molecular dynamics. Biochemistry 26:8012-8013.
8. Erickson JC, Sewell AK, Jensen LT, Winge DR, Palmiter RD. 1994. Enhanced neurotrophic activity in Alzheimer's disease cortex is not associated with down-regulation of metallothionein-III (GIF). Brain Res 649:297-304.
9. Jeener J, Meier BH, Bachmann P, Ernst RR. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 71:4546-4563.
10. Kägi JHR, Kojima Y. 1987. Chemistry and biochemistry of metallothionein. In: Kägi JHR, Kojima Y, eds. Metallothionein II. Basel: Birkhäuser Verlag. pp 25-61.
11. Kägi JHR, Schärfer A. 1988. Biochemistry of metallothionein. Biochemistry 27:8509-8515.
12. 113Cd NMR spectroscopy of the solid and implications for cadmiumthiolate ligation in proteins. Inorg Chem 23:930-935.
13. + binding to metallothionein. Biochemistry 35:13929-13936.
14. Messerle B, Bos M, Schäffer A, Vašak M, Kägi JHR, Wüthrich K. 1990a. Amide proton exchange in human metallothionein-2 measured by nuclear magnetic resonance spectroscopy. J Mol Biol 214:781-786.
15. 7] metallothionein-2 in aqueous solution determined by nuclear magnetic resonance spectroscopy. J Mol Biol 214:765-779.
16. 7]-metallothionein-2 using nuclear magnetic resonance spectroscopy. J Mol Biol 225:433-443.
17. Müller L. 1979. Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence. J Am Chem Soc 101:4481-4484.
18. Narula SS, Brouwer M, Hua Y, Armitage IM. 1995. Three-dimensional structure of callinectes sapidus metallothionein-1 determined by homonuclear and heteronuclear magnetic resonance spectroscopy. Biochemistry 34:620-631.
19. Nicholls A, Sharp K, Honig B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
20. Nilges M, Clore GM, Gronenborn AM. 1988. Determination of the three-dimensional structures of proteins from interprotons distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Lett 229:317-329.
21. Otvos JD, Engeseth HR, Nettesheim DG, Hilt CR. 1987. Interprotein metal exchange reactions of metallothionein. In: Metallothionein II. Basel: Birkhäuser Verlag, pp 171-178.
22. Piotto M, Saudek V, Sklenar V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661-665.
23. Robbins AH, McRee DE, Williamson M, Collet SA, Xuong NH, Furey WF, Wang BC, Stout CD. 1991. Refined crystal structure of Cd.Zn metallothionein at 2.0 Å resolution. J Mol Biol 221:1269-1293.
24. 7]-melallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy. Biochemistry 203:251-268.
25. Shaka AJ, Barker PB, Freeman R. 1985. Computer-optimised decoupling scheme for wideband application and low-level operation. J Magn Reson 64:547-552.
26. Shaka AJ, Lee CJ, Pines A. 1988. Iterative schemes for bilinear operators: Application to spin decoupling. J Magn Reson 77:274-293.
27. States DJ, Haberkorn RA, Ruben DJ. 1982. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J Magn Reson 48:286-292.
28. 2 (M = Mn(II), Ni(II), Zn(II), Cd(II). Inorg Chem 24:2820-2826.
29. 1H nuclear magnetic resonance and distance geometry. J Mol Biol 182:295-315.
30. 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135-140.
31. Wüthrich K. 1986. NMR of proteins and nucleic acids. New York: John Wiley & Sons.
32. Zangger K, Armitage IM. 1999. The accordion HMQC. Heteronuclear correlation for a range of coupling constants. J Magn Reson. Forthcoming.