4.6 Article

Structural approaches to probing metal interaction with proteins

Journal

JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 115, Issue -, Pages 138-147

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2012.02.015

Keywords

Amyloid precursor protein; Glutathione transferase; Insulin-regulated aminopeptidase; X-ray absorption spectroscopy; X-ray crystallography

Funding

  1. National Health and Medical Research Council of Australia (NHMRC) Dora Lush Scholarship
  2. International Centre for Diffraction Data Crystallography Scholarship
  3. Colin North and Major Engineering

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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. (C) 2012 Elsevier Inc. All rights reserved.

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