D2 dopamine receptor homodimerization is mediated by multiple sites of interaction, including an intermolecular interaction involving transmembrane domain 4

Biochemistry

Volumn 42, Issue 37, 2003, Pages 11023-11031

  Lee, Samuel P ^a   O'Dowd, Brian F ^a,b   Rajaram, Ryan D ^a   Nguyen, Tuan ^a,b   George, Susan R ^a,b,c  

^a UNIVERSITY OF TORONTO   (Canada)

^b CENTRE FOR ADDICTION AND MENTAL HEALTH   (Canada)

^c UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

DIMERIZATION; HYDROPHOBICITY; MUTAGENESIS; OLIGOMERS; PROTEINS;

INTERMOLECULAR INTERACTIONS;

BIOCHEMISTRY;

DIMER; DOPAMINE 1 RECEPTOR; DOPAMINE 2 RECEPTOR; OLIGOMER;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIMERIZATION; DISSOCIATION; HORMONE RECEPTOR INTERACTION; HYDROPHOBICITY; IMMUNOBLOTTING; MEMBRANE STRUCTURE; MOLECULAR INTERACTION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; RECEPTOR OCCUPANCY; TRANSMEMBRANE DOMAIN 4;

ANIMALS; BINDING SITES; CELL LINE; CELL MEMBRANE; COS CELLS; DIMERIZATION; DISULFIDES; DNA, COMPLEMENTARY; GENE DELETION; GENETIC VECTORS; GLYCOSYLATION; HUMANS; IMMUNOBLOTTING; INSECTS; KINETICS; MUTATION; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, DOPAMINE; REDUCING AGENTS;

ANIMALIA;

EID: 0141431029     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0345539     Document Type: Article

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