The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: Analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F

Journal of Biological Chemistry

Volumn 279, Issue 35, 2004, Pages 36363-36371

  Morgan, Clinton T ^a   Tsivkovskii, Ruslan ^a   Kosinsky, Yuri A ^b   Efremov, Roman G ^b   Lutsenko, Svetlana ^a,b  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; DISEASES; METABOLISM; PROTEINS; TITRATION;

HUMAN METABOLISM; WILSON DISEASE (WD);

ADENOSINETRIPHOSPHATE;

ADENOSINE TRIPHOSPHATASE; COPPER; COPPER EXPORTING ADENOSINE TRIPHOSPHATASE; NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; WILSON DISEASE PROTEIN;

ARTICLE; BINDING AFFINITY; CALORIMETRY; DISEASE SEVERITY; ENZYME ANALYSIS; GENE DISRUPTION; GENE MUTATION; HUMAN; HUMAN CELL; ISOTHERMAL TITRATION CALORIMETRY; METAL BINDING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; REDUCTION; STATISTICAL SIGNIFICANCE; STRUCTURE ACTIVITY RELATION; WILSON DISEASE;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ARGININE; CALORIMETRY; CATION TRANSPORT PROTEINS; CIRCULAR DICHROISM; CYSTEINE; GLUTAMIC ACID; HISTIDINE; HUMANS; KINETICS; MAGNESIUM; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; NUCLEOTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; TEMPERATURE;

EID: 4344689863     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M404553200     Document Type: Article

References (33)

1. Lutsenko, S., Efremov, R. G., Tsivkovskii, R., and Walker, J. M. (2002) J. Bioenerg. Biomembr. 34, 351-362
2. Fatemi, N., and Sarkar, B. (2002) J. Bioenerg. Biomembr. 34, 339-349
3. Lutsenko, S., and Petris, M. J. (2003) J. Membr. Biol. 191, 1-12
4. Gitlin, J. D. (2003) Gastroenterology 125, 1868-1877
5. Loudianos, G., and Gitlin, J. D. (2000) Semin. Liver Dis. 20, 353-364
6. Riordan, S. M., and Williams, R. (2001) J. Hepatol. 34, 165-171
7. Cox, D. W., and Moore, S. D. (2002) J. Bioenerg. Biomembr. 34, 333-338
8. Katano, K., Safaei, R., Samimi, G., Holzer, A., Rochdi, M., and Howell, S. B. (2003) Mol. Pharmacol. 64, 466-473
9. Nakayama, K., Kanzaki, A., Ogawa, K., Miyazaki, K., Neamati, N., and Takebayashi, Y. (2002) Int. J. Cancer 101, 488-495
10. Komatsu, M., Sumizawa, T., Mutoh, M., Chen, Z. S., Terada, K., Furukawa, T., Yang, X. L., Gao, H., Miura, N., Sugiyama, T., and Akiyama, S. (2000) Cancer Res. 60, 1312-1316
11. Tsivkovskii, R., Eisses, J. F., Kaplan, J. H., and Lutsenko, S. (2002) J. Biol. Chem. 277, 976-983
12. Toyoshima, C., and Nomura, H. (2002) Nature 418, 605-611
13. Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Nature 405, 647-655
14. Toyoshima, C., Nomura, H., and Sugita, Y. (2003) FEBS Lett. 555, 106-110
15. Clausen, J. D., Vilsen, B., McIntosh, D. B., Einholm, A. P., and Andersen, J. P. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 2776-2781
16. Axelsen, K. B., and Palmgren, M. G. (1998) J. Mol. Evol. 46, 84-101
17. Lutsenko, S., and Kaplan, J. H. (1995) Biochemistry 34, 15607-15613
18. Bissig, K. D., Wunderli-Ye, H., Duda, P. W., and Solioz, M. (2001) Biochem. J. 357, 217-223
19. Okkeri, J., Bencomo, E., Pietila, M., and Haltia, T. (2002) Eur. J. Biochem. 269, 1579-1586
20. Okkeri, J., Laakkonen, L., and Haltia, T. (2004) Biochem. J. 377, 95-105
21. Voskoboinik, I., Mar, J., and Camakaris, J. (2003) Biochem. Biophys. Res. Commun. 301, 488-494
22. Tsivkovskii, R., Efremov, R. G., and Lutsenko, S. (2003) J. Biol. Chem. 278, 13302-13308
23. Sreerama, N., and Woody, R. W. (2000) Anal. Biochem. 287, 252-260
24. Efremov, R. G., Kosinsky Y. A., Nolde, D. E., Tsivkovskii, R., Arseniev, A. S., Lutsenko, S. (May 17, 2004) Biochem. J. [Epub ahead of print]
25. Efremov, R. G., Vergoten, G. (1995) J. Phys. Chem. 99, 10658-10666
26. Hilge, M., Siegal, G., Vuister, G. W., Guntert, P., Gloor, S. M., and Abrahams, J. P. (2003) Nat. Struct. Biol. 10, 468-474
27. Champeil, P., Menguy, T., Soulie, S., Juul, B., de Gracia, A. G., Rusconi, F., Falson, P., Denoroy, L., Henao, F., le Maire, M., and Moller, J. V. (1998) J. Biol. Chem. 273, 6619-6631
28. Abu-Abed, M., Millet, O., MacLennan, D. H., and Ikura, M. (2004) Biochem. J. 379, 235-242
29. Gatto, C., Wang, A. X., and Kaplan, J. H. (1998) J. Biol. Chem. 273, 10578-10585
30. Loudianos, G., Dessi, V., Lovicu, M., Angius, A., Altuntas, B., Giacchino, R., Marazzi, M., Marcellini, M., Sartorelli, M. R., Sturniolo, G. C., Kocak, N., Yuce, A., Akar, N., Pirastu, M., and Cao, A. (1999) J. Med. Genet. 36, 833-836
31. Solioz, M., and Vulpe, C. (1996) Trends Biochem. Sci. 21, 237-241
32. Tsivkovskii, R., MacArthur, B. C., and Lutsenko, S. (2001) J. Biol. Chem. 276, 2234-2242
33. Deleted in press.