Functional roles of transiently and intrinsically disordered regions within proteins
Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well‐folded structures. Even small, well‐folded single‐domain proteins are structurally heterogeneous and contain multiple foldon...
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| Published in | The FEBS journal Vol. 282; no. 7; pp. 1182 - 1189 |
|---|---|
| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
England
Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies
01.04.2015
Blackwell Publishing Ltd |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1742-464X 1742-4658 1742-4658 |
| DOI | 10.1111/febs.13202 |
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| Abstract | Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well‐folded structures. Even small, well‐folded single‐domain proteins are structurally heterogeneous and contain multiple foldon units with different conformational stability. Although the ability of many intrinsically disordered protein regions to undergo at least partial folding at interaction with specific binding partners is a well‐established fact, recent studies have revealed that functions of some ordered proteins rely on the decrease in the amount of their ordered structure and require local or even global functional unfolding. This functional unfolding is induced by transient alterations in protein environment or by modification of protein structure and can be reversed as soon as the environment is restored or the modification is removed. Therefore, the important features of these conditionally disordered protein regions (or unfoldons) are the induced nature and the transient character of their disorder. In other words, structurally any protein can be described as a modular assembly of foldons, inducible foldons, semi‐foldons, nonfoldons and unfoldons. Obviously, differently ordered/disordered proteins and protein regions can possess very different functional repertoires. This review represents some of the key functions of transiently and intrinsically disordered protein regions. |
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| AbstractList | Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well-folded structures. Even small, well-folded single-domain proteins are structurally heterogeneous and contain multiple foldon units with different conformational stability. Although the ability of many intrinsically disordered protein regions to undergo at least partial folding at interaction with specific binding partners is a well-established fact, recent studies have revealed that functions of some ordered proteins rely on the decrease in the amount of their ordered structure and require local or even global functional unfolding. This functional unfolding is induced by transient alterations in protein environment or by modification of protein structure and can be reversed as soon as the environment is restored or the modification is removed. Therefore, the important features of these conditionally disordered protein regions (or unfoldons) are the induced nature and the transient character of their disorder. In other words, structurally any protein can be described as a modular assembly of foldons, inducible foldons, semi-foldons, nonfoldons and unfoldons. Obviously, differently ordered/disordered proteins and protein regions can possess very different functional repertoires. This review represents some of the key functions of transiently and intrinsically disordered protein regions.Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well-folded structures. Even small, well-folded single-domain proteins are structurally heterogeneous and contain multiple foldon units with different conformational stability. Although the ability of many intrinsically disordered protein regions to undergo at least partial folding at interaction with specific binding partners is a well-established fact, recent studies have revealed that functions of some ordered proteins rely on the decrease in the amount of their ordered structure and require local or even global functional unfolding. This functional unfolding is induced by transient alterations in protein environment or by modification of protein structure and can be reversed as soon as the environment is restored or the modification is removed. Therefore, the important features of these conditionally disordered protein regions (or unfoldons) are the induced nature and the transient character of their disorder. In other words, structurally any protein can be described as a modular assembly of foldons, inducible foldons, semi-foldons, nonfoldons and unfoldons. Obviously, differently ordered/disordered proteins and protein regions can possess very different functional repertoires. This review represents some of the key functions of transiently and intrinsically disordered protein regions. Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well‐folded structures. Even small, well‐folded single‐domain proteins are structurally heterogeneous and contain multiple foldon units with different conformational stability. Although the ability of many intrinsically disordered protein regions to undergo at least partial folding at interaction with specific binding partners is a well‐established fact, recent studies have revealed that functions of some ordered proteins rely on the decrease in the amount of their ordered structure and require local or even global functional unfolding. This functional unfolding is induced by transient alterations in protein environment or by modification of protein structure and can be reversed as soon as the environment is restored or the modification is removed. Therefore, the important features of these conditionally disordered protein regions (or unfoldons) are the induced nature and the transient character of their disorder. In other words, structurally any protein can be described as a modular assembly of foldons, inducible foldons, semi‐foldons, nonfoldons and unfoldons. Obviously, differently ordered/disordered proteins and protein regions can possess very different functional repertoires. This review represents some of the key functions of transiently and intrinsically disordered protein regions. Structure of any protein can be described as a modular assembly of foldons, inducible foldons, semi‐foldons, nonfoldons, and unfoldons possessing very different functional repertoires. Therefore, not only ordered or completely disordered proteins, but also proteins and protein regions with different shades of order and different flavors of disorder are functional, generating a unique protein structure‐function continuum. Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well-folded structures. Even small, well-folded single-domain proteins are structurally heterogeneous and contain multiple foldon units with different conformational stability. Although the ability of many intrinsically disordered protein regions to undergo at least partial folding at interaction with specific binding partners is a well-established fact, recent studies have revealed that functions of some ordered proteins rely on the decrease in the amount of their ordered structure and require local or even global functional unfolding. This functional unfolding is induced by transient alterations in protein environment or by modification of protein structure and can be reversed as soon as the environment is restored or the modification is removed. Therefore, the important features of these conditionally disordered protein regions (or unfoldons) are the induced nature and the transient character of their disorder. In other words, structurally any protein can be described as a modular assembly of foldons, inducible foldons, semi-foldons, nonfoldons and unfoldons. Obviously, differently ordered/disordered proteins and protein regions can possess very different functional repertoires. This review represents some of the key functions of transiently and intrinsically disordered protein regions. |
| Author | Uversky, Vladimir N |
| Author_xml | – sequence: 1 fullname: Uversky, Vladimir N |
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| Snippet | Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that... |
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| SubjectTerms | foldon induced foldon intrinsically disordered protein Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - physiology intrinsically disordered region Molecular biology molecular recognition nonfoldon post‐translational modification protein binding Protein Folding Protein Structure, Tertiary proteins protein–protein interaction semi‐foldon unfoldon |
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| Title | Functional roles of transiently and intrinsically disordered regions within proteins |
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