Protein Conformational Switches: From Nature to Design
Identifieur interne : 000440 ( Istex/Checkpoint ); précédent : 000439; suivant : 000441Protein Conformational Switches: From Nature to Design
Auteurs : Jeung-Hoi Ha ; Stewart N. Loh [États-Unis]Source :
- Chemistry – A European Journal [ 0947-6539 ] ; 2012-06-25.
Abstract
Protein conformational switches alter their shape upon receiving an input signal, such as ligand binding, chemical modification, or change in environment. The apparent simplicity of this transformation—which can be carried out by a molecule as small as a thousand atoms or so—belies its critical importance to the life of the cell as well as its capacity for engineering by humans. In the realm of molecular switches, proteins are unique because they are capable of performing a variety of biological functions. Switchable proteins are therefore of high interest to the fields of biology, biotechnology, and medicine. These molecules are beginning to be exploited as the core machinery behind a new generation of biosensors, functionally regulated enzymes, and “smart” biomaterials that react to their surroundings. As inspirations for these designs, researchers continue to analyze existing examples of allosteric proteins. Recent years have also witnessed the development of new methodologies for introducing conformational change into proteins that previously had none. Herein we review examples of both natural and engineered protein switches in the context of four basic modes of conformational change: rigid‐body domain movement, limited structural rearrangement, global fold switching, and folding–unfolding. Our purpose is to highlight examples that can potentially serve as platforms for the design of custom switches. Accordingly, we focus on inducible conformational changes that are substantial enough to produce a functional response (e.g., in a second protein to which it is fused), yet are relatively simple, structurally well‐characterized, and amenable to protein engineering efforts.
Protein shape‐shifters: Protein conformational switches are able to transform their 3D shapes in response to stimuli. This shape‐shifting ability is innate to some proteins and it can be engineered into others. Conformational switching is an often‐hidden aspect of protein structure that is emerging as the core machinery behind a new generation of biosensors and other smart materials that react to their surroundings.
Url:
DOI: 10.1002/chem.201200348
Affiliations:
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Loh</name><affiliation></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation><affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Chemistry – A European Journal</title><title level="j" type="alt">CHEMISTRY - A EUROPEAN JOURNAL</title><idno type="ISSN">0947-6539</idno><idno type="eISSN">1521-3765</idno><imprint><biblScope unit="vol">18</biblScope><biblScope unit="issue">26</biblScope><biblScope unit="page" from="7984">7984</biblScope><biblScope unit="page" to="7999">7999</biblScope><biblScope unit="page-count">16</biblScope><publisher>WILEY‐VCH Verlag</publisher><pubPlace>Weinheim</pubPlace><date type="published" when="2012-06-25">2012-06-25</date></imprint><idno type="ISSN">0947-6539</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0947-6539</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein conformational switches alter their shape upon receiving an input signal, such as ligand binding, chemical modification, or change in environment. The apparent simplicity of this transformation—which can be carried out by a molecule as small as a thousand atoms or so—belies its critical importance to the life of the cell as well as its capacity for engineering by humans. In the realm of molecular switches, proteins are unique because they are capable of performing a variety of biological functions. Switchable proteins are therefore of high interest to the fields of biology, biotechnology, and medicine. These molecules are beginning to be exploited as the core machinery behind a new generation of biosensors, functionally regulated enzymes, and “smart” biomaterials that react to their surroundings. As inspirations for these designs, researchers continue to analyze existing examples of allosteric proteins. Recent years have also witnessed the development of new methodologies for introducing conformational change into proteins that previously had none. Herein we review examples of both natural and engineered protein switches in the context of four basic modes of conformational change: rigid‐body domain movement, limited structural rearrangement, global fold switching, and folding–unfolding. Our purpose is to highlight examples that can potentially serve as platforms for the design of custom switches. Accordingly, we focus on inducible conformational changes that are substantial enough to produce a functional response (e.g., in a second protein to which it is fused), yet are relatively simple, structurally well‐characterized, and amenable to protein engineering efforts.</div><div type="abstract" xml:lang="en">Protein shape‐shifters: Protein conformational switches are able to transform their 3D shapes in response to stimuli. This shape‐shifting ability is innate to some proteins and it can be engineered into others. Conformational switching is an often‐hidden aspect of protein structure that is emerging as the core machinery behind a new generation of biosensors and other smart materials that react to their surroundings.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Ha, Jeung Oi" sort="Ha, Jeung Oi" uniqKey="Ha J" first="Jeung-Hoi" last="Ha">Jeung-Hoi Ha</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Loh, Stewart N" sort="Loh, Stewart N" uniqKey="Loh S" first="Stewart N." last="Loh">Stewart N. Loh</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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