Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β2-adrenergic receptor-Reference-Cited by-同舟云学术

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Structural and functional roles of small group-conserved amino acids present on helix-H7 in the β2-adrenergic receptor

Published:2011-04 Issue:4 Volume:1808 Page:1170-1178
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Arakawa Makoto,Chakraborty Raja,Upadhyaya Jasbir,Eilers Markus,Reeves Philip J.,Smith Steven O.,Chelikani Prashen

Funder

Canadian Institute of Health Research

Manitoba Health Research Council

NIH

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference37 articles.

1. Cloning of the gene and cDNA for mammalian β-adrenergic receptor and homology with rhodopsin;Dixon;Nature,1986

2. High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor;Cherezov;Science,2007

3. Structure of bovine rhodopsin in a trigonal crystal form;Li;J. Mol. Biol.,2004

4. Crystal structure of rhodopsin: a G protein-coupled receptor;Palczewski;Science,2000

5. Comparison of helix interactions in membrane and soluble α-bundle proteins;Eilers;Biophys. J.,2002

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1. Structural basis for receptor selectivity and inverse agonism in S1P5 receptors;Nature Communications;2022-08-12

2. Evolutionary association of receptor-wide amino acids with G protein–coupling selectivity in aminergic GPCRs;Life Science Alliance;2022-05-25

3. Structural basis for receptor selectivity and inverse agonism in S1P₅ receptors;2022-02-26

4. Receptor-wide Determinants of G Protein Coupling Selectivity in Aminergic GPCRs;2021-09-17

5. A Conserved Proline Hinge Mediates Helix Dynamics and Activation of Rhodopsin;Structure;2020-09

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