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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Small-molecule control of protein function through Staudinger reduction.

Ji Luo1, Qingyang Liu1, Kunihiko Morihiro1

  • 1Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.

Nature Chemistry
|October 22, 2016
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel small-molecule switch to precisely control protein activity in live cells. This method uses bioorthogonal Staudinger reduction for site-specific protein activation, enabling conditional control over cellular processes.

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Area of Science:

  • Chemical Biology
  • Molecular and Cellular Biology
  • Biotechnology

Background:

  • Controlling protein function in live cells with high specificity is a significant challenge in biological research.
  • Existing methods often lack precision or are difficult to implement in complex cellular environments.

Purpose of the Study:

  • To develop a novel small-molecule-based system for the conditional control of protein activity in mammalian cells.
  • To enable site-specific inactivation and subsequent activation of proteins using bioorthogonal chemistry.

Main Methods:

  • Genetically encoding an ortho-azidobenzyloxycarbonyl amino acid into proteins using a pyrrolysyl transfer RNA synthetase/tRNACUA pair.
  • Utilizing a phosphine-mediated Staudinger reduction for bioorthogonal deprotection and protein activation.
  • Site-specific introduction of a small-molecule-removable protecting group to render proteins inactive.

Main Results:

  • Demonstrated successful conditional control of protein activity through site-specific deprotection.
  • Validated the methodology across diverse cellular functions, including bioluminescence, fluorescence, protein translocation, DNA recombination, and gene editing (Cas9).
  • Achieved precise temporal and spatial control over protein function in live mammalian cells.

Conclusions:

  • The developed small-molecule switch provides a powerful and versatile tool for precise control of protein function.
  • This bioorthogonal approach offers significant advantages for studying dynamic biological processes and developing targeted therapeutics.
  • The methodology is broadly applicable to various proteins and cellular systems, opening new avenues in chemical biology and synthetic biology.