Abstract
Cyanovirin-N (CV-N), an 11-kDa protein from the cyanobacterium Nostoc ellipsosporum, is a highly potent virucidal agent that has generated interest as a lead natural product for the prevention and chemotherapy of human immunodeficiency virus infection. The antiviral activity of CV-N is mediated through specific, high-affinity interactions with the viral surface envelope glycoproteins. A number of structures of wild-type, mutant and sequence-shuffled CV-N have been solved by nuclear magnetic resonance and crystallography, showing that the protein exists as either a quasi-symmetric two-domain monomer or a domain-swapped dimer. Structures of several complexes of CV-N with oligosaccharides help in explaining the unique mode of high-affinity binding of these molecules to both forms of CV-N.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Anti-HIV Agents / chemistry
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Anti-HIV Agents / therapeutic use
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Bacterial Proteins / therapeutic use
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Carrier Proteins / therapeutic use
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Crystallography, X-Ray
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Dimerization
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HIV Envelope Protein gp120 / drug effects
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HIV Envelope Protein gp120 / metabolism
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HIV Infections / drug therapy
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HIV Infections / prevention & control
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HIV-1 / drug effects
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Humans
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Imaging, Three-Dimensional
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Structure
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Mutation
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Protein Structure, Tertiary
Substances
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Anti-HIV Agents
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Bacterial Proteins
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Carrier Proteins
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HIV Envelope Protein gp120
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cyanovirin N