Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase

Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase Mammalian Genome 11, 409–411 (2000). Incorporating Mouse Genome © Springer-Verlag New York Inc. 2000 Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase 1 1 1 2 2 Thomas B. Bartnikas, Darrel J. Waggoner, Ruby Leah B. Casareno, Roger Gaedigk, Robert A. White, Jonathan D. Gitlin Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri, USA Section of Medical Genetics and Molecular Medicine, The Children’s Mercy Hospital, Kansas City, Missouri, USA Received: 5 October 1999 / Accepted: 27 January 2000 The delivery of copper to specific targets within the cell is medi- the crystal structure of S. cerevisiae CCS (yCCS) (Lamb et al. ated by a distinct group of intracellular carrier proteins termed 1999), reveal that CCS consists of three domains: an amino- metallochaperones. CCS, the copper chaperone for cytosolic cop- terminal domain I, an internal domain II exhibiting significant per/zinc superoxide dismutase (SOD1), has been identified in yeast homology to SOD1, and a carboxy-terminal domain III. Domain I and humans and is necessary and sufficient for copper incorpora- contains a putative copper-binding motif, MXCXXC, that is sur- tion into SOD1 in vivo (Culotta et al. 1997; Rae et al. 1999). CCS prisingly http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Mammalian Genome Springer Journals

Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase

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Publisher
Springer-Verlag
Copyright
Copyright © 2000 by Springer-Verlag New York Inc.
Subject
Life Sciences; Cell Biology; Animal Genetics and Genomics; Human Genetics
ISSN
0938-8990
eISSN
1432-1777
D.O.I.
10.1007/s003350010078
Publisher site
See Article on Publisher Site

Abstract

Mammalian Genome 11, 409–411 (2000). Incorporating Mouse Genome © Springer-Verlag New York Inc. 2000 Chromosomal localization of CCS, the copper chaperone for Cu/Zn superoxide dismutase 1 1 1 2 2 Thomas B. Bartnikas, Darrel J. Waggoner, Ruby Leah B. Casareno, Roger Gaedigk, Robert A. White, Jonathan D. Gitlin Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri, USA Section of Medical Genetics and Molecular Medicine, The Children’s Mercy Hospital, Kansas City, Missouri, USA Received: 5 October 1999 / Accepted: 27 January 2000 The delivery of copper to specific targets within the cell is medi- the crystal structure of S. cerevisiae CCS (yCCS) (Lamb et al. ated by a distinct group of intracellular carrier proteins termed 1999), reveal that CCS consists of three domains: an amino- metallochaperones. CCS, the copper chaperone for cytosolic cop- terminal domain I, an internal domain II exhibiting significant per/zinc superoxide dismutase (SOD1), has been identified in yeast homology to SOD1, and a carboxy-terminal domain III. Domain I and humans and is necessary and sufficient for copper incorpora- contains a putative copper-binding motif, MXCXXC, that is sur- tion into SOD1 in vivo (Culotta et al. 1997; Rae et al. 1999). CCS prisingly

Journal

Mammalian GenomeSpringer Journals

Published: May 1, 2000

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