Copper-Binding Properties of X-linked Inhibitor of Apoptosis Protein (XIAP) and Putative Complex Formation with Metallochaperone for Cu,Zn-Superoxide Dismutase Protein (CCS)

Authors

Yiwen Liang, Macalester College

Document Type

Honors Project On-Campus Access Only

Abstract

Copper is an essential trace metal in biological systems and it is regulated via a homeostatic system of copper binding proteins. Malfunction of this system resulting in copper toxicity is linked to many severe human diseases. XIAP was newly identified to be a copper binding protein and was implicated to interact with CCS via complex formation. In this study, XIAP domain BIR23 was found to bind up to three copper ions and three cysteine residues are key in the copper binding process. Evidence also suggests BIR23 dimerization following copper binding. The interaction between CCS and XIAP was probed with various techniques.

Recommended Citation

Liang, Yiwen, "Copper-Binding Properties of X-linked Inhibitor of Apoptosis Protein (XIAP) and Putative Complex Formation with Metallochaperone for Cu,Zn-Superoxide Dismutase Protein (CCS)" (2013). Chemistry Honors Projects. 12.
https://digitalcommons.macalester.edu/chem_honors/12