The fourth transmembrane segment forms the interface of the dopamine D2 receptor homodimer

Journal of Biological Chemistry

Volumn 278, Issue 7, 2003, Pages 4385-4388

  Guo, Wen ^a   Shi, Lei ^a   Javitch, Jonathan A ^a,b  

^a Columbia Univ Coll of Phys/Surgs ^*  (United States)

^b Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOLOGICAL MEMBRANES; DIMERS; INTERFACES (MATERIALS); PROTEINS;

LIGAND BINDING;

BIOCHEMISTRY;

CYSTEINE; DIMER; DOPAMINE 2 RECEPTOR; G PROTEIN COUPLED RECEPTOR; CROSS LINKING REAGENT; LIGAND;

ARTICLE; CONTROLLED STUDY; CROSS LINKING; DIMERIZATION; EMBRYO; HUMAN; HUMAN CELL; IN VIVO STUDY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN STRUCTURE; BINDING SITE; CELL MEMBRANE; CHEMISTRY; GENETICS; METABOLISM; MUTATION; SIGNAL TRANSDUCTION;

BINDING SITES; CELL MEMBRANE; CROSS-LINKING REAGENTS; CYSTEINE; HUMANS; LIGANDS; MUTATION; RECEPTORS, DOPAMINE D2; SIGNAL TRANSDUCTION;

EID: 0038576278     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.C200679200     Document Type: Article

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