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Structure, properties, and engineering of the major zinc binding site on human albumin
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Blindauer, Claudia A., Harvey, Ian, Bunyan, Kerry E., Stewart, Alan J., Sleep, Darrell, Harrison, David J., Berezenko, Stephen and Sadler, P. J. (2009) Structure, properties, and engineering of the major zinc binding site on human albumin. Journal of Biological Chemistry, Vol.284 (No.34). pp. 23116-23124. doi:10.1074/jbc.M109.003459 ISSN 0021-9258.
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Official URL: http://dx.doi.org/10.1074/jbc.M109.003459
Abstract
Most blood plasma zinc is bound to albumin, but the structure of the binding site has not been determined. Zn K-edge extended x-ray absorption fine structure spectroscopy and modeling studies show that the major Zn2+ site on albumin is a 5-coordinate site with average Zn-O/N distances of 1.98 angstrom and a weak sixth O/N bond of 2.48 angstrom, consistent with coordination to His(67) and Asn(99) from domain I, His(247) and Asp(249) from domain II (residues conserved in all sequenced mammalian albumins), plus a water ligand. The dynamics of the domain I/II interface, thought to be important to biological function, are affected by Zn2+ binding, which induces cooperative allosteric effects related to those of the pH-dependent neutral-to-base transition. N99D and N99H mutations enhance Zn2+ binding but alter protein stability, whereas mutation of His67 to alanine removes an interdomain H-bond and weakens Zn2+ binding. Both wildtype and mutant albumins promote the safe management of high micromolar zinc concentrations for cells in cultures.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||
| Library of Congress Subject Headings (LCSH): | Albumins, Zinc, Cooperative binding (Biochemistry), Chemical affinity | ||||
| Journal or Publication Title: | Journal of Biological Chemistry | ||||
| Publisher: | American Society for Biochemistry and Molecular Biology, Inc. | ||||
| ISSN: | 0021-9258 | ||||
| Official Date: | 21 August 2009 | ||||
| Dates: |
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| Volume: | Vol.284 | ||||
| Number: | No.34 | ||||
| Number of Pages: | 9 | ||||
| Page Range: | pp. 23116-23124 | ||||
| DOI: | 10.1074/jbc.M109.003459 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Royal Society (Great Britain), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Novozymes Biopharma, Ltd, European Community Marie Curie Fellowship, Wellcome Trust (London, England), Wolfson Foundation |
Data sourced from Thomson Reuters' Web of Knowledge
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