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Affinity and specificity of motif-based protein-protein interactions

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TLDR
Recent advances in molecular aspects of affinity and specificity in protein-protein interactions involving disordered protein regions are reviewed.
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This article is published in Current Opinion in Structural Biology.The article was published on 2019-02-01 and is currently open access. It has received 78 citations till now. The article focuses on the topics: Binding site & Protein–protein interaction.

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Interactions by Disorder - A Matter of Context.

TL;DR: This review emphasizes how multivalency, charges and charge clusters, hydrophobic patches, dynamics, energetic frustration, and ensemble redistribution of flanking regions or disordered contexts are emerging as important contributors to allosteric regulation, positive and negative cooperativity, feedback regulation and negative selection in binding.
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The functional importance of structure in unstructured protein regions.

TL;DR: The current understanding of different types of intramolecular IDR interactions, their effects on IDR complex formation and their modes of biological regulation are reviewed.
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The pathobiology of perturbed mutant huntingtin protein-protein interactions in Huntington's disease.

TL;DR: This review focuses on abnormal PPIs that are associated with the assembly of mutant HTT aggregates in cells and their potential relevance in disease, and discusses the mechanisms and pathobiological processes that may contribute to phenotype development, neuronal dysfunction and toxicity in Huntington's disease brains.
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Quantitative mapping of protein-peptide affinity landscapes using spectrally encoded beads.

TL;DR: This work systematically probes binding of calcineurin (CN), a conserved protein phosphatase essential for the immune response and target of immunosuppressants, and discovers that flanking residues and post-translational modifications critically contribute to PxIxIT-CN affinity.
References
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Journal ArticleDOI

Intrinsically disordered proteins in cellular signalling and regulation.

TL;DR: Experimental, computational and bioinformatic analyses combine to identify and characterize disordered regions of proteins, leading to a greater appreciation of their widespread roles in biological processes.
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Transcriptional activation by recruitment

TL;DR: Findings from experiments in bacteria and yeast indicate that many genes can be activated by the recruitment model for gene activation, and for the role of histones in gene regulation.
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A conserved docking motif in MAP kinases common to substrates, activators and regulators

TL;DR: A hitherto unidentified docking motif in MAPKs is revealed that is used in common for recognition of their activators, substrates and regulators and increases the efficiency of the enzymatic reactions.
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Scaffold Proteins: Hubs for Controlling the Flow of Cellular Information

TL;DR: Although most scaffolds use a simple tethering mechanism to increase the efficiency of interaction between individual partner molecules, these proteins can also exert complex allosteric control over their partners and are themselves the target of regulation.
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