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Nature of cation-π interactions and their role in structural stability of immunoglobulin proteins

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Abstract

Cation-π interactions are known to be important contributors to protein stability and ligand-protein interactions. In this study, we have analyzed the influence of cation-π interactions in single chain immunoglobulin proteins. We observed 87 cation-π interactions in a data set of 33 proteins. These interactions are mainly formed by long-range contacts, and there is preference of Arg over Lys in these interactions. Arg-Tyr interactions are predominant among the various pairs analyzed. Despite the scarcity of interactions involving Trp, the average energy for Trp-cation interactions is quite high. This information suggests that the cation-π interactions involving Trp might be of high relevance to the proteins. Secondary structure analysis reveals that cation-π interactions are formed preferably between residues in which at least one is in β-strand. Proteins having β-strand regions have the highest number of cation-π interaction-forming residues.

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Abbreviations

ASA:

accessible surface area

LRO:

long-range order

SC:

stabilizing centers

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Authors and Affiliations

  1. Bioinformatics Division, School of Biosciences and Technology, Vellore Institute of Technology, Vellore, 632014, Tamil Nadu, India

    I. A. Tayubi & R. Sethumadhavan

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  1. I. A. Tayubi
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  2. R. Sethumadhavan
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Correspondence to R. Sethumadhavan.

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Tayubi, I.A., Sethumadhavan, R. Nature of cation-π interactions and their role in structural stability of immunoglobulin proteins. Biochemistry Moscow 75, 912–918 (2010). https://doi.org/10.1134/S000629791007014X

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  • DOI: https://doi.org/10.1134/S000629791007014X

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