PubMed:12678493 JSONTXT

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":285,"end":301},"obj":"HP_0002721"}],"text":"Cyanovirin-N: a sugar-binding antiviral protein with a new twist.\nCyanovirin-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."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":87,"end":92},"obj":"gene:10238"},{"id":"T1","span":{"begin":279,"end":317},"obj":"disease:C0019693"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Cyanovirin-N: a sugar-binding antiviral protein with a new twist.\nCyanovirin-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."}

{"project":"Lectin_function","denotations":[{"id":"T1","span":{"begin":0,"end":12},"obj":"GL_000336"},{"id":"T2","span":{"begin":30,"end":39},"obj":"FN_000009"},{"id":"T3","span":{"begin":66,"end":78},"obj":"GL_000336"},{"id":"T4","span":{"begin":323,"end":332},"obj":"FN_000009"}],"text":"Cyanovirin-N: a sugar-binding antiviral protein with a new twist.\nCyanovirin-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."}