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|Title:||Structural approaches to probing metal interaction with proteins|
|Citation:||Journal of Inorganic Biochemistry, 2012; 115:138-147|
|Publisher:||Elsevier Science Inc|
|Lorien J. Parker, David B. Ascher, Chen Gao, Luke A. Miles, Hugh H. Harris, Michael W. Parker|
|Abstract:||In this mini-review we focus on metal interactions with proteins with a particular emphasis on the evident synergism between different biophysical approaches toward understanding metallobiology. We highlight three recent examples from our own laboratory. Firstly, we describe metallodrug interactions with glutathione S-transferases, an enzyme family known to attack commonly used anti-cancer drugs. We then describe a protein target for memory enhancing drugs called insulin-regulated aminopeptidase in which zinc plays a role in catalysis and regulation. Finally we describe our studies on a protein, amyloid precursor protein, that appears to play a central role in Alzheimer's disease. Copper ions have been implicated in playing both beneficial and detrimental roles in the disease by binding to different regions of this protein.|
|Keywords:||Amyloid precursor protein; Glutathione transferase; Insulin-regulated aminopeptidase; X-ray absorption spectroscopy; X-ray crystallography|
|Rights:||Copyright © 2012 Elsevier Inc. All rights reserved.|
|Appears in Collections:||Chemistry publications|
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