A structural insight into the reorientation of transmembrane domains 3 and 5 during family A GPCR activation

K. Sansuk; X. Deupi; I. Torrecillas; A. Jongejan; S. Nijmeijer; R.A. Bakker; L. Pardo; R. Leurs

doi:10.1124/mol.110.066068

A structural insight into the reorientation of transmembrane domains 3 and 5 during family A GPCR activation

K. Sansuk, X. Deupi, I. Torrecillas, A. Jongejan, S. Nijmeijer, R.A. Bakker, L. Pardo, R. Leurs

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Rearrangement of transmembrane domains (TMs) 3 and 5 after agonist binding is necessary for stabilization of the active state of class A G protein-coupled receptors (GPCRs). Using sitedirected mutagenesis and functional assays, we provide the first evidence that the TAS(I/V) sequence motif at positions 3.37 to 3.40, highly conserved in aminergic receptors, plays a key role in the activation of the histamine H

Original language	English
Journal	Molecular Pharmacology
DOIs	https://doi.org/10.1124/mol.110.066068
Publication status	Published - 2010

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title = "A structural insight into the reorientation of transmembrane domains 3 and 5 during family A GPCR activation",

abstract = "Rearrangement of transmembrane domains (TMs) 3 and 5 after agonist binding is necessary for stabilization of the active state of class A G protein-coupled receptors (GPCRs). Using sitedirected mutagenesis and functional assays, we provide the first evidence that the TAS(I/V) sequence motif at positions 3.37 to 3.40, highly conserved in aminergic receptors, plays a key role in the activation of the histamine H",

author = "K. Sansuk and X. Deupi and I. Torrecillas and A. Jongejan and S. Nijmeijer and R.A. Bakker and L. Pardo and R. Leurs",

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T1 - A structural insight into the reorientation of transmembrane domains 3 and 5 during family A GPCR activation

AU - Sansuk, K.

AU - Deupi, X.

AU - Torrecillas, I.

AU - Jongejan, A.

AU - Nijmeijer, S.

AU - Bakker, R.A.

AU - Pardo, L.

AU - Leurs, R.

PY - 2010

Y1 - 2010

N2 - Rearrangement of transmembrane domains (TMs) 3 and 5 after agonist binding is necessary for stabilization of the active state of class A G protein-coupled receptors (GPCRs). Using sitedirected mutagenesis and functional assays, we provide the first evidence that the TAS(I/V) sequence motif at positions 3.37 to 3.40, highly conserved in aminergic receptors, plays a key role in the activation of the histamine H

AB - Rearrangement of transmembrane domains (TMs) 3 and 5 after agonist binding is necessary for stabilization of the active state of class A G protein-coupled receptors (GPCRs). Using sitedirected mutagenesis and functional assays, we provide the first evidence that the TAS(I/V) sequence motif at positions 3.37 to 3.40, highly conserved in aminergic receptors, plays a key role in the activation of the histamine H

U2 - 10.1124/mol.110.066068

DO - 10.1124/mol.110.066068

M3 - Article

JO - Molecular pharmacology

JF - Molecular pharmacology

SN - 0026-895X

ER -

A structural insight into the reorientation of transmembrane domains 3 and 5 during family A GPCR activation

Abstract

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