Lysine-60 in Copper Chaperone Atox1 Plays an Essential Role in Adduct Formation with a Target Wilson Disease Domain-Reference-Cited by-同舟云学术

Lysine-60 in Copper Chaperone Atox1 Plays an Essential Role in Adduct Formation with a Target Wilson Disease Domain

Published:2009-10-28 Issue:45 Volume:131 Page:16371-16373
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hussain Faiza¹,Rodriguez-Granillo Agustina¹,Wittung-Stafshede Pernilla¹

Affiliation:

1. Department of Biochemistry and Cell Biology, Rice University, 6100 Main Street, Houston, Texas 77251, and Department of Chemistry, Chemical Biological Center, Umeå University, 901 87 Umeå, Sweden

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9058266

Reference12 articles.

1. Metallochaperones and Metal-Transporting ATPases: A Comparative Analysis of Sequences and Structures

2. Solution Structure of the Apo and Copper(I)-Loaded Human Metallochaperone HAH1

3. Conserved residues modulate copper release in human copper chaperone Atox1

4. Differential Roles of Met10, Thr11, and Lys60 in Structural Dynamics of Human Copper Chaperone Atox1

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