beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations

S J Sanni; J T Hansen; M M Bonde; T Speerschneider; G L Christensen; S Munk; S Gammeltoft; J L Hansen

doi:10.1111/j.1476-5381.2010.00875.x

beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations

S J Sanni, J T Hansen, M M Bonde, T Speerschneider, G L Christensen, S Munk, S Gammeltoft, J L Hansen

Afdeling for Klinisk Biokemi

25 Citationer (Scopus)

Abstract

The angiotensin II type 1 (AT(1)) receptor belongs to family A of 7 transmembrane (7TM) receptors. The receptor has important roles in the cardiovascular system and is commonly used as a drug target in cardiovascular diseases. Interaction of 7TM receptors with G proteins or beta-arrestins often induces higher binding affinity for agonists. Here, we examined interactions between AT(1A) receptors and beta-arrestins to look for differences between the AT(1A) receptor interaction with beta-arrestin1 and beta-arrestin2.

Originalsprog	Engelsk
Tidsskrift	British Journal of Pharmacology
Vol/bind	161
Udgave nummer	1
Sider (fra-til)	150-61
Antal sider	12
ISSN	0007-1188
DOI	https://doi.org/10.1111/j.1476-5381.2010.00875.x
Status	Udgivet - 1 sep. 2010

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10.1111/j.1476-5381.2010.00875.x

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abstract = "The angiotensin II type 1 (AT(1)) receptor belongs to family A of 7 transmembrane (7TM) receptors. The receptor has important roles in the cardiovascular system and is commonly used as a drug target in cardiovascular diseases. Interaction of 7TM receptors with G proteins or beta-arrestins often induces higher binding affinity for agonists. Here, we examined interactions between AT(1A) receptors and beta-arrestins to look for differences between the AT(1A) receptor interaction with beta-arrestin1 and beta-arrestin2.",

author = "Sanni, {S J} and Hansen, {J T} and Bonde, {M M} and T Speerschneider and Christensen, {G L} and S Munk and S Gammeltoft and Hansen, {J L}",

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doi = "10.1111/j.1476-5381.2010.00875.x",

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T1 - beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations

AU - Sanni, S J

AU - Hansen, J T

AU - Bonde, M M

AU - Speerschneider, T

AU - Christensen, G L

AU - Munk, S

AU - Gammeltoft, S

AU - Hansen, J L

PY - 2010/9/1

Y1 - 2010/9/1

N2 - The angiotensin II type 1 (AT(1)) receptor belongs to family A of 7 transmembrane (7TM) receptors. The receptor has important roles in the cardiovascular system and is commonly used as a drug target in cardiovascular diseases. Interaction of 7TM receptors with G proteins or beta-arrestins often induces higher binding affinity for agonists. Here, we examined interactions between AT(1A) receptors and beta-arrestins to look for differences between the AT(1A) receptor interaction with beta-arrestin1 and beta-arrestin2.

AB - The angiotensin II type 1 (AT(1)) receptor belongs to family A of 7 transmembrane (7TM) receptors. The receptor has important roles in the cardiovascular system and is commonly used as a drug target in cardiovascular diseases. Interaction of 7TM receptors with G proteins or beta-arrestins often induces higher binding affinity for agonists. Here, we examined interactions between AT(1A) receptors and beta-arrestins to look for differences between the AT(1A) receptor interaction with beta-arrestin1 and beta-arrestin2.

U2 - 10.1111/j.1476-5381.2010.00875.x

DO - 10.1111/j.1476-5381.2010.00875.x

M3 - Journal article

C2 - 20718747

SN - 0007-1188

VL - 161

SP - 150

EP - 161

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

IS - 1

ER -

beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations

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