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Ligand-induced rearrangement of the dimeric metabotropic glutamate receptor 1alpha.

Abstract：

:The extracellular domain of the metabotropic glutamate receptor 1alpha (mGluR1alpha) forms a dimer and the ligand, glutamate, induces a structural rearrangement in this domain. However, the conformational change in the cytoplasmic domain, which is critical for mGluR1alpha's interaction with G proteins, remains unclear. Here we investigated the ligand-induced conformational changes in the cytoplasmic domain by fluorescence resonance energy transfer (FRET) analysis of mGluR1alpha labeled with fluorescent protein(s) under total internal reflection field microscopy. Upon ligand binding, the intersubunit FRET efficiency between the second loops increased, whereas that between first loops decreased. In contrast, the intrasubunit FRET did not change clearly. These results show that ligand binding does not change the structure of each subunit, but does change the dimeric allocation of the cytoplasmic regions, which may underlie downstream signaling.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Tateyama M,Abe H,Nakata H,Saito O,Kubo Y

doi

10.1038/nsmb770

keywords:

subject

Has Abstract

pub_date

2004-07-01 00:00:00

pages

637-42

issue

7

eissn

1545-9993

issn

1545-9985

pii

nsmb770

journal_volume

11

pub_type

杂志文章

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