Crystal structure of a fully glycosylated HIV-1 gp 120 core reveals a stabilizing role for the glycan at Asn262

Proteins: Structure, Function and Bioinformatics

Volumn 83, Issue 3, 2015, Pages 590-596

  Kong, Leopold ^a,b   Wilson, Ian A ^b   Kwong, Peter D ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Glycan shield; HIV 1 gp120; Role of N262

Indexed keywords

GLYCAN; GLYCOPROTEIN GP 120; MANNOSE OLIGOSACCHARIDE; NEUTRALIZING ANTIBODY; ASPARAGINE; CD4 ANTIGEN; MANNOSE; POLYSACCHARIDE;

ARTICLE; CRYSTAL STRUCTURE; ELECTRON; HUMAN IMMUNODEFICIENCY VIRUS 1; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; ANTIBODY COMBINING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GLYCOSYLATION; HEK293 CELL LINE; HUMAN; METABOLISM; X RAY CRYSTALLOGRAPHY;

HUMAN IMMUNODEFICIENCY VIRUS 1;

ANTIGENS, CD4; ASPARAGINE; BINDING SITES, ANTIBODY; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLATION; HEK293 CELLS; HIV ENVELOPE PROTEIN GP120; HIV-1; HUMANS; MANNOSE; MODELS, MOLECULAR; POLYSACCHARIDES;

EID: 84922496561     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24747     Document Type: Article

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