ChimeSquare.comTM Chime SquareTM Animations Molecular Graphics Resource

Eric C. Niederhoffer, Ph.D. Ecnhoffer@chimesquare.com Copyright 2000- , E.C. Niederhoffer. All Rights Reserved. All trademarks and copyrights are the property of their respective owners.

Yeast (Saccharomyces cerevisiae) copper chaperone for Sod (1qup), human copper chaperone for Sod (1do5), and human copper,zinc-superoxide dismutase (1spd)

• What structural elements are present in each molecule?
• What is the subunit composition?
• What comparisons exist with the structures?

Lamb, A. L., A. K. Wernimont, R. A. Pufahl, T. V. O'Halloran, and A. C. Rosenzweig. 1999. Crystal structure of the copper chaperone for superoxide dismutase Nat. Struct. Biol. 6:724-729.

Lamb, A. L., A. K. Wernimont, R. A. Pufahl, T. V. O'Halloran, and A. C. Rosenzweig. 2000. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry 39:1589-1595.

Deng, H. X., A. Hentati, J. A. Tainer, Z. Iqbal, A. Cayabyab, W. Y. Hung, E. D. Getzoff, P. Hu, B. Herzfeldt, R. P. Roos, C. Warner, G. Deng, E. Soriano, C. Smyth, H. E. Parge, A. Ahmed, A. D. Roses, R. A. Hallewell, M. A. Pericak-Vance, and T. Siddique. 1993. Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261:1047-1051.

chimesquare.com