期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 278, 期 7, 页码 4385-4388出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C200679200
关键词
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资金
- NIMH NIH HHS [MH57324, MH54137] Funding Source: Medline
Considerable evidence suggests that G-protein-coupled receptors form homomeric and heteromeric dimers in vivo. Unraveling the structural mechanism for crosstalk between receptors in a dimeric complex must start with the identification of the presently unknown dimer interface. Here, by using cysteine cross-linking, we identify the fourth transmembrane segment (TM4) as a symmetrical dimer interface in the dopamine D2 receptor. Cross-linking is unaffected by ligand binding, and ligand binding and receptor activation are unaffected by cross-linking, suggesting that the receptor is a constitutive dimer. The accessibility of adjacent residues in TM4, however, is affected by ligand binding, implying that the interface has functional significance.
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