Dimerization of the calcium-sensing receptor occurs within the extracellular domain and is eliminated by Cys → Ser mutations at Cys101 and Cys236

Journal of Biological Chemistry

Volumn 274, Issue 17, 1999, Pages 11629-11634

  Pace, Amy J ^a   Gama, Lucio ^a   Breitwieser, Gerda E ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GREEN FLUORESCENT PROTEIN; SERINE;

AMINO ACID SUBSTITUTION; ARTICLE; CALCIUM CELL LEVEL; CALCIUM TRANSPORT; COVALENT BOND; DIMERIZATION; DISULFIDE BOND; EXTRACELLULAR CALCIUM; GLYCOSYLATION; HUMAN; HUMAN CELL; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; RECEPTOR AFFINITY;

BASE SEQUENCE; CELL LINE; CYSTEINE; DIMERIZATION; DISULFIDES; DNA PRIMERS; GREEN FLUORESCENT PROTEINS; HUMANS; LUMINESCENT PROTEINS; POINT MUTATION; RECEPTORS, CALCIUM-SENSING; RECEPTORS, CELL SURFACE; SERINE;

EID: 0033597249     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.17.11629     Document Type: Article

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