Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins (Q40628650)

22 September 2017

title

Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins (English)

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22 September 2017

4

Vsevolod V Gurevich

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22 September 2017

author name string

Sergey A Vishnivetskiy

series ordinal

1

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22 September 2017

M Marlene Hosey

series ordinal

2

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22 September 2017

Jeffrey L Benovic

series ordinal

3

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22 September 2017

language of work or name

English

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publication date

6 October 2003

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Journal of Biological Chemistry

22 September 2017

published in

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22 September 2017

volume

279

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22 September 2017

issue

2

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22 September 2017

page(s)

1262-1268

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Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin.

22 September 2017

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Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge

21 January 2018

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21 January 2018

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21 January 2018

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Interaction of arrestins with intracellular domains of muscarinic and alpha2-adrenergic receptors.

21 January 2018

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Regulated interactions of the alpha 2A adrenergic receptor with spinophilin, 14-3-3zeta, and arrestin 3.

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Functionally different agonists induce distinct conformations in the G protein coupling domain of the beta 2 adrenergic receptor

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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A segment corresponding to amino acids Val170-Arg182 of bovine arrestin is capable of binding to phosphorylated rhodopsin.

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase

21 January 2018

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Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes

21 January 2018

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Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: sulfhydryl reactivity and transducin activation reveal a tertiary structure

21 January 2018

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Insertional mutagenesis and immunochemical analysis of visual arrestin interaction with rhodopsin

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M308834200

1 reference

22 September 2017

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