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5K79

Structure and anti-HIV activity of CYT-CVNH, a new cyanovirin-n homolog

Summary for 5K79
Entry DOI10.2210/pdb5k79/pdb
DescriptorCyanovirin-N domain protein, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordssugar binding lectin, hiv-inactivating, antiviral protein, oligosaccharide
Biological sourceCyanothece sp. (strain PCC 7424)
Total number of polymer chains2
Total formula weight24146.15
Authors
Matei, E.,Basu, R.,Furey, W.,Shi, J.,Calnan, C.,Aiken, C.,Gronenborn, A.M. (deposition date: 2016-05-25, release date: 2016-07-20, Last modification date: 2024-11-13)
Primary citationMatei, E.,Basu, R.,Furey, W.,Shi, J.,Calnan, C.,Aiken, C.,Gronenborn, A.M.
Structure and Glycan Binding of a New Cyanovirin-N Homolog.
J.Biol.Chem., 291:18967-18976, 2016
Cited by
PubMed Abstract: The HIV-1 envelope glycoprotein gp120 is heavily glycosylated and bears numerous high mannose sugars. These sugars can serve as targets for HIV-inactivating compounds, such as antibodies and lectins, which bind to the glycans and interfere with viral entry into the target cell. We determined the 1.6 Å x-ray structure of Cyt-CVNH, a recently identified lectin from the cyanobacterium Cyanothece(7424), and elucidated its glycan specificity by NMR. The Cyt-CVNH structure and glycan recognition profile are similar to those of other CVNH proteins, with each domain specifically binding to Manα(1-2)Manα units on the D1 and D3 arms of high mannose glycans. However, in contrast to CV-N, no cross-linking and precipitation of the cross-linked species in solution was observed upon Man-9 binding, allowing, for the first time, investigation of the interaction of Man-9 with a member of the CVNH family by NMR. HIV assays showed that Cyt-CVNH is able to inhibit HIV-1 with ∼4-fold higher potency than CV-N(P51G), a stabilized version of wild type CV-N. Therefore, Cyt-CVNH may qualify as a valuable lectin for potential microbicidal use.
PubMed: 27402833
DOI: 10.1074/jbc.M116.740415
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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