Design and engineering of allosteric communications in proteins |
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Affiliation: | 1. Department of Pharmacology, Penn State College of Medicine, Hershey, PA, 17033-0850, USA;2. Department of Biochemistry & Molecular Biology, Penn State College of Medicine, Hershey, PA, 17033-0850, USA;3. Department of Chemistry, Pennsylvania State University, University Park, PA, 16802, USA;4. Department of Biomedical Engineering, Pennsylvania State University, University Park, PA, 16802, USA;1. Department of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida;2. School of Pharmacy, State Key Laboratory of Applied Organic Chemistry and Department of Chemistry, Lanzhou University, Lanzhou, China;1. Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC, 27599, USA;2. Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, 27514, USA |
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Abstract: | Allostery in proteins plays an important role in regulating protein activities and influencing many biological processes such as gene expression, enzyme catalysis, and cell signaling. The process of allostery takes place when a signal detected at a site on a protein is transmitted via a mechanical pathway to a functional site and, thus, influences its activity. The pathway of allosteric communication consists of amino acids that form a network with covalent and non-covalent bonds. By mutating residues in this allosteric network, protein engineers have successfully established novel allosteric pathways to achieve desired properties in the target protein. In this review, we highlight the most recent and state-of-the-art techniques for allosteric communication engineering. We also discuss the challenges that need to be overcome and future directions for engineering protein allostery. |
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Keywords: | MD" },{" #name" :" keyword" ," $" :{" id" :" pc_QN9RHFnjnK" }," $$" :[{" #name" :" text" ," _" :" molecular dynamics NMR" },{" #name" :" keyword" ," $" :{" id" :" pc_xAiRQIuH81" }," $$" :[{" #name" :" text" ," _" :" nuclear magnetic resonance TROSY" },{" #name" :" keyword" ," $" :{" id" :" pc_SFiEnnqB9o" }," $$" :[{" #name" :" text" ," _" :" transverse relaxation optimized spectroscopy GPCR" },{" #name" :" keyword" ," $" :{" id" :" pc_6371L6DRgq" }," $$" :[{" #name" :" text" ," _" :" G protein-coupled receptor FAK" },{" #name" :" keyword" ," $" :{" id" :" pc_JpRBZC5wJe" }," $$" :[{" #name" :" text" ," _" :" focal adhesion kinase |
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