Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines

Journal of Experimental Medicine

Volumn 194, Issue 11, 2001, Pages 1661-1673

  Bannert, Norbert ^a,b   Craig, Stewart ^a,b   Farzan, Michael ^a,b   Sogah, Dodzie ^a,b   Santo, Niki Villanueva ^a,b   Choe, Hyeryun ^b,c   Sodroski, Joseph ^a,b,d  

^a DANA FARBER CANCER INSTITUTE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c BOSTON CHILDREN S HOSPITAL   (United States)

^d HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

CCR5; HIV; O Glycosylation; Sialic acid; Tyrosine sulfation

Indexed keywords

CHEMOKINE; CHEMOKINE RECEPTOR CCR5; GLYCAN DERIVATIVE; OLIGOSACCHARIDE; SELECTIN; THREONINE; TYROSINE; TYROSINE DERIVATIVE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; DOG; GLYCOSYLATION; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SULFATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; CELL LINE, TRANSFORMED; CELLS, CULTURED; CHO CELLS; CRICETINAE; DOGS; GENE EXPRESSION; GLYCOSYLATION; HELA CELLS; HIV-1; HUMANS; MACROPHAGE INFLAMMATORY PROTEIN-1; MACROPHAGES; MOLECULAR SEQUENCE DATA; N-ACETYLNEURAMINIC ACID; POLYSACCHARIDES; PROTEIN BINDING; RECEPTORS, CCR5; SIMIAN IMMUNODEFICIENCY VIRUS; SULFATES; TYROSINE;

EID: 0035803466     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.194.11.1661     Document Type: Article

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