Structural Basis of Arrestin Selectivity for Active Phosphorylated G Protein-Coupled Receptors (original) (raw)

Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation

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The structural basis of the arrestin binding to GPCRs

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Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide

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Molecular mechanism of phosphorylation-dependent arrestin activation

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Few Residues within an Extensive Binding Interface Drive Receptor Interaction and Determine the Specificity of Arrestin Proteins

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Receptor-Arrestin Interactions: The GPCR Perspective

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Functional map of arrestin-1 at single amino acid resolution

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Role of Receptor-attached Phosphates in Binding of Visual and Non-visual Arrestins to G Protein-coupled Receptors

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Transition of Arrestin into the Active Receptor-binding State Requires an Extended Interdomain Hinge

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An Additional Phosphate-binding Element in Arrestin Molecule. IMPLICATIONS FOR THE MECHANISM OF ARRESTIN ACTIVATION

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Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes

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Differential manipulation of arrestin-3 binding to basal and agonist-activated G protein-coupled receptors

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The Role of Arrestin α-Helix I in Receptor Binding

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Conservation of the Phosphate-sensitive Elements in the Arrestin Family of Proteins

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Conformational sensors and domain-swapping reveal structural and functional differences between β-arrestin isoforms

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How Does Arrestin Respond to the Phosphorylated State of Rhodopsin?

Sergey Vishnivetskiy

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Arrestin Variants Display Differential Binding Characteristics for the Phosphorylated N-Formyl Peptide Receptor Carboxyl Terminus

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Functional map of arrestin binding to phosphorylated opsin, with and without agonist

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The Role of Arrestin-1 Middle Loop in Rhodopsin Binding

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Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction

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The arrestin-1 finger loop interacts with two distinct conformations of active rhodopsin

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Arrestins: Introducing Signaling Bias Into Multifunctional Proteins

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Partial Phosphorylation of the N-Formyl Peptide Receptor Inhibits G Protein Association Independent of Arrestin Binding

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Extensive shape shifting underlies functional versatility of arrestins

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Phosphate Sensor and Construction of Phosphorylation-Independent Arrestins

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Molecular Determinants Underlying the Formation of Stable Intracellular G Protein-coupled Receptor-β-Arrestin Complexes after Receptor Endocytosis*

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