Circulatory zinc transport is controlled by distinct interdomain sites on mammalian albumins-Reference-Cited by-同舟云学术

Circulatory zinc transport is controlled by distinct interdomain sites on mammalian albumins

Published:2016 Issue:11 Volume:7 Page:6635-6648
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Handing Katarzyna B.¹²³⁴⁵^ORCID,Shabalin Ivan G.¹²³⁴⁵^ORCID,Kassaar Omar⁶⁷⁸⁹,Khazaipoul Siavash⁶⁷⁸⁹,Blindauer Claudia A.¹⁰¹¹¹²⁹^ORCID,Stewart Alan J.⁶⁷⁸⁹^ORCID,Chruszcz Maksymilian¹³¹⁴¹⁵⁴^ORCID,Minor Wladek¹²³⁴⁵^ORCID

Affiliation:

1. Department of Molecular Physiology and Biological Physics

2. University of Virginia School of Medicine

3. Charlottesville

4. USA

5. New York Structural Genomics Research Consortium (NYSGRC)

6. School of Medicine

7. University of St. Andrews

8. St. Andrews KY16 9TF

9. UK

10. Department of Chemistry

11. University of Warwick

12. Coventry CV4 7AL

13. Department of Chemistry and Biochemistry

14. University of South Carolina

15. Columbia

Abstract

Circulatory transport of the essential nutrient zinc primarily occurs through its binding to serum albumin. Here, we present the first crystal structures of mammalian albumins in complex with zinc. These structures, together with accompanying zinc binding data, allow identification of key zinc transport sites on human and equine albumins.

Funder

British Heart Foundation

National Institutes of Health

Biotechnology and Biological Sciences Research Council

Michigan Economic Development Corporation

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/SC/C6SC02267G

Reference65 articles.