Protein-Cation Interactions: Structural and Thermodynamic Aspects

Author(s): X. Arias-Moreno , O. Abian , S. Vega , J. Sancho , A. Velazquez-Campoy .

Journal Name: Current Protein & Peptide Science

Volume 12 , Issue 4 , 2011

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Abstract:

Cations are specifically recognized by numerous proteins. Cations may play a structural role, as cofactors stabilizing their binding partners, or a functional role, as cofactors activating their binding partners or being themselves involved in enzymatic reactions. Despite their small size, their charge density and their specific interaction with highly charged residues allow them to induce significant conformational changes on their binding proteins. The protein conformational change induced by cation binding may be as large as to account for the complete folding of a protein (as evidenced in Hepatitis C NS3 protease, or human rhinovirus 2A protease), and they may also trigger oligomerization (as in calcium-binding protein 1). Especially intriguing is the ability of cation-binding proteins of discriminating between very similar cations. In particular, calcium and magnesium are recognized by proteins with markedly different binding affinities and cause significantly different conformational changes and stabilization effects in the binding proteins (as in the fifth ligand binding repeat of the LDL receptor binding domain, calcium-binding protein 1, or parvalbumin). This article summarizes recent findings on the structural and energetic impact of cation binding to different proteins. A general framework can be envisaged in which cations can be considered as a special type of allosteric effectors able to modulate the functional properties of proteins, in particular the ability to interact with biological targets, by altering their conformational equilibrium.

Keywords: Cation binding, protein-ligand interaction, protein stability, conformational change, thermodynamics, calorimetry, stabilization effects, proteins, enzymatic reactiond

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Article Details

VOLUME: 12
ISSUE: 4
Year: 2011
Page: [325 - 338]
Pages: 14
DOI: 10.2174/138920311795906664
Price: $58

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