Structure and Conformational Changes in the C-terminal Domain of the β2-Adrenoceptor-Reference-Cited by-同舟云学术

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Structure and Conformational Changes in the C-terminal Domain of the β2-Adrenoceptor

Published:2007-05 Issue:18 Volume:282 Page:13895-13905
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Granier Seébastien,Kim Samuel,Shafer Aaron M.,Ratnala Venkata R.P.,Fung Juan Joseé,Zare Richard N.,Kobilka Brian

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. G Protein-coupled Receptors

2. Structural Mimicry in G Protein-Coupled Receptors: Implications of the High-Resolution Structure of Rhodopsin for Structure-Function Analysis of Rhodopsin-Like Receptors

3. Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin

4. Structural Features and Light-Dependent Changes in the Sequence 306−322 Extending from Helix VII to the Palmitoylation Sites in Rhodopsin: A Site-Directed Spin-Labeling Study,

5. 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,

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1. Exploring GPCR conformational dynamics using single-molecule fluorescence;Methods;2024-06

2. Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction;Structure;2023-11

3. Function and dynamics of the intrinsically disordered carboxyl terminus of β2 adrenergic receptor;Nature Communications;2023-04-10

4. Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction;2023-02-23

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