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Probing New and Underexplored Protein-Protein Interactions

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (30 April 2020) | Viewed by 2945

Special Issue Editor

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Guest Editor
Division of Medicinal Chemistry, Department of Pharmaceutical Sciences, School of Pharmacy, University of Connecticut, Storrs, CT 06269, USA
Interests: drug discovery and development; assay design; compound screening; protein–protein interactions; computational medicinal chemistry; cancer; chemical biology
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Special Issue Information

Dear Colleagues,

Protein-protein interactions (PPIs) are essential for the proper biological function of almost every process that occurs inside a cell. As such, a clear understanding of as many PPIs as possible is key for understanding normal and aberrant cellular signaling. Multiple approaches have been utilized to probe both individual PPIs and larger protein interaction networks. Techniques such as tandem affinity purification, protein–fragment complementation, and coimmunoprecipitation are commonly used to identify protein interaction partners in vitro. Structural biology (NMR, x-ray crystallography, cryo-EM) can determine key intermolecular interactions at the interface of a PPI and identify hotspot regions essential for binding. Combining this structural information with cellular mutation studies provides insight into how disruption of a PPI affects its biological function. In addition, the development of small-molecule PPI inhibitors as chemical probes and potential drugs has greatly enhanced our understanding of the therapeutic potential of PPIs. Finally, in silico methods have proven capable of predicting PPIs and exploring the dynamic changes the protein partners undergo during the binding process. This Special Issue will consider for publication reviews and original research articles that focus on utilizing these and other related techniques to expand our knowledge on new and underexplored PPIs. 

Assoc. Prof. M. Kyle Hadden
Guest Editor

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  • Protein-Protein Interactions
  • Structural Biology
  • Chemical Probes
  • In Silico Methods
  • Mutational Studies

Published Papers (1 paper)

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12 pages, 1141 KiB  
Probing the Protein-Protein Interaction between the ATRXADD Domain and the Histone H3 Tail
by Angela M. Zaino, Radha Charan Dash and M. Kyle Hadden
Molecules 2020, 25(7), 1500; - 25 Mar 2020
Viewed by 2687
While loss-of-function mutations in the ATRX gene have been implicated as a driving force for a variety of pediatric brain tumors, as well as pancreatic neuroendocrine tumors, the role of ATRX in gene regulation and oncogenic development is not well-characterized. The ADD domain [...] Read more.
While loss-of-function mutations in the ATRX gene have been implicated as a driving force for a variety of pediatric brain tumors, as well as pancreatic neuroendocrine tumors, the role of ATRX in gene regulation and oncogenic development is not well-characterized. The ADD domain of ATRX (ATRXADD) localizes the protein to chromatin by specifically binding to the histone H3 tail. This domain is also a primary region that is mutated in these cancers. The overall goal of our studies was to utilize a variety of techniques (experimental and computational) to probe the H3:ATRXADD protein-protein interaction (PPI). We developed two biochemical assays that can be utilized to study the interaction. These assays were utilized to experimentally validate and expand upon our previous computational results. We demonstrated that the three anchor points in the H3 tail (A1, K4, and K9) are all essential for high affinity binding and that disruption of more than one contact region will be required to develop a small molecule that disrupts the PPI. Our approach in this study could be applied to other domains of ATRX, as well as PPIs between other distinct proteins. Full article
(This article belongs to the Special Issue Probing New and Underexplored Protein-Protein Interactions)
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