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Frankel, Alan D.

doi:10.1038/70002

Cited by 28 publications

(17 citation statements)

References 32 publications

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“…In the case of RNA-protein complexes, induced fit upon binding can be seen in either the RNA or the protein components 1 . The free protein and/or RNA may have a disordered or flexible region, or simply a different conformation than the bound form.…”

Section: Induced Fit In Rna-protein Complexesmentioning

confidence: 99%

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2000

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Two generalizations can be drawn from the recent rapid progress in understanding RNA-protein interactions. First, there is a great diversity of observed protein and RNA structural motifs. Second, formation of almost every RNA-protein complex that has been characterized involves conformational changes in the protein, the RNA, or both. The role of these conformational changes in the biological function of RNA-protein complexes is not at all clear. Whether or not conformational changes are a critical feature of ribonucleoprotein complex assembly or are an unimportant mechanistic detail, the ubiquity of these changes warrants careful consideration of their implications.

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Section: Induced Fit In Rna-protein Complexesmentioning

confidence: 99%

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2000

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“…Other specific contacts between single‐stranded RNA loops and proteins are often mediated by aromatic amino acids. In any case, induced fit of either one or both binding partners is very frequently observed in RNA–protein recognition and is mechanistically important for biological regulation 6–9…”

Section: Aromatic Peptide Motifs Selected With Rna Structures Derivedmentioning

confidence: 99%

Identification of Peptide Ligands for Target RNA Structures Derived from the HIV‐1 Packaging Signal ψ by Screening Phage‐Displayed Peptide Libraries

et al. 2003

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Tying up the package: The HIV‐1 RNA packaging signal ψ is a complex RNA structure located within the 5′‐end of unspliced HIV‐1 RNAs (see picture). Upon binding of the viral polyprotein Gag to the ψ RNA, a process mediated by the nucleocapsid protein NCp7, two RNA genomes are packaged into the assembling virions. By using phage display technology peptides were selected that bind specifically to different RNA structures derived from the ψ RNA.

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“…As a consequence of conformational flexibility, these proteins often go through binding-induced folding[ 5 ]. Such disorder-to-order transitions appear ubiquitously, and in RNA-protein interactions conformational changes can occur either in the structure of the protein, the RNA partner, or both [ 6 ]. However, disorder-to-order transitions entail special energetic consequences on the interaction, because a fraction of the available binding enthalpy needs to compensate for the entropic cost of the conformational changes [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins

et al. 2015

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Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder have never been fully assessed. Here, through large-scale analysis of comprehensive protein sequence and structure datasets we demonstrate the prevalence of intrinsic structural disorder in RNA-binding proteins and domains. We addressed their functionality through a quantitative description of the evolutionary conservation of disordered segments involved in binding, and investigated the structural implications of flexibility in terms of conformational stability and interface formation. We conclude that the functional role of intrinsically disordered protein segments in RNA-binding is two-fold: first, these regions establish extended, conserved electrostatic interfaces with RNAs via induced fit. Second, conformational flexibility enables them to target different RNA partners, providing multi-functionality, while also ensuring specificity. These findings emphasize the functional importance of intrinsically disordered regions in RNA-binding proteins.

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Cited by 28 publications

References 32 publications

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Identification of Peptide Ligands for Target RNA Structures Derived from the HIV‐1 Packaging Signal ψ by Screening Phage‐Displayed Peptide Libraries

Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins

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