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Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase: In Silico Approach to Identify PPI Inhibitors

Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase: In Silico Approach to Identify PPI Inhibitors

Sailu Sarvagalla, Mohane Selvaraj Coumar
Copyright: © 2017 |Pages: 29
ISBN13: 9781522517627|ISBN10: 1522517626|EISBN13: 9781522517634
DOI: 10.4018/978-1-5225-1762-7.ch043
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MLA

Sarvagalla, Sailu, and Mohane Selvaraj Coumar. "Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase: In Silico Approach to Identify PPI Inhibitors." Pharmaceutical Sciences: Breakthroughs in Research and Practice, edited by Information Resources Management Association, IGI Global, 2017, pp. 1115-1143. https://doi.org/10.4018/978-1-5225-1762-7.ch043

APA

Sarvagalla, S. & Coumar, M. S. (2017). Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase: In Silico Approach to Identify PPI Inhibitors. In I. Management Association (Ed.), Pharmaceutical Sciences: Breakthroughs in Research and Practice (pp. 1115-1143). IGI Global. https://doi.org/10.4018/978-1-5225-1762-7.ch043

Chicago

Sarvagalla, Sailu, and Mohane Selvaraj Coumar. "Protein-Protein Interactions (PPIs) as an Alternative to Targeting the ATP Binding Site of Kinase: In Silico Approach to Identify PPI Inhibitors." In Pharmaceutical Sciences: Breakthroughs in Research and Practice, edited by Information Resources Management Association, 1115-1143. Hershey, PA: IGI Global, 2017. https://doi.org/10.4018/978-1-5225-1762-7.ch043

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Abstract

Most of the developed kinase inhibitor drugs are ATP competitive and suffer from drawbacks such as off-target kinase activity, development of resistance due to mutation in the ATP binding pocket and unfavorable intellectual property situations. Besides the ATP binding pocket, protein kinases have binding sites that are involved in Protein-Protein Interactions (PPIs); these PPIs directly or indirectly regulate the protein kinase activity. Of recent, small molecule inhibitors of PPIs are emerging as an alternative to ATP competitive agents. Rational design of inhibitors for kinase PPIs could be carried out using molecular modeling techniques. In silico tools available for the prediction of hot spot residues and cavities at the PPI sites and the means to utilize this information for the identification of inhibitors are discussed. Moreover, in silico studies to target the Aurora B-INCENP PPI sites are discussed in context. Overall, this chapter provides detailed in silico strategies that are available to the researchers for carrying out structure-based drug design of PPI inhibitors.

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