Solution structure of a circular-permuted variant of the potent HIV-inactivating protein cyanovirin-N: Structural basis for protein stability and oligosaccharide interaction

Journal of Molecular Biology

Volumn 325, Issue 1, 2003, Pages 211-223

  Barrientos, Laura G ^a   Louis, John M ^a   Ratner, Daniel M ^b   Seeberger, Peter H ^b   Gronenborn, Angela M ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Circular permuted CV N; Cyanovirin N; gp120; High mannose sugars; Protein carbohydrate interaction

Indexed keywords

AMIDE; CARBOHYDRATE DERIVATIVE; CYANOVIRIN N; EPITOPE; GLYCINE; GLYCOPROTEIN GP 120; MANNOSE; OLIGOSACCHARIDE; PROLINE; PROTEIN WT; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANTIVIRAL ACTIVITY; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; DRUG INTERACTION; DRUG POTENCY; HYDROGEN BOND; HYDROPHOBICITY; MUTATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; VIRUS INACTIVATION; WILD TYPE;

EID: 0037258662     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01205-6     Document Type: Article

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