5k79

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

spinqualitylabelsall models 5k79, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5k79 is a 2 chain structure with sequence from Gloeothece citriformis PCC 7424. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: EDO, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7KDN5_GLOC7 Publication Abstract from PubMed 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 A X-ray structure of Cyt-CVNH, a recently identified lectin from the cyanobacterium Cyanothece7424, 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 Mana(1-2)Mana 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 solutions was observed upon Man-9 binding, allowing for the first time to investigate 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-NP51G, a stabilized version of wild type CV-N. Therefore, Cyt-CVNH may qualify as a valuable lectin for potential microbicidal use. Structure and Glycan Binding of a New Cyanovirin-N Homolog.,Matei E, Basu R, Furey W, Shi J, Calnan C, Aiken C, Gronenborn AM J Biol Chem. 2016 Jul 7. pii: jbc.M116.740415. PMID:27402833 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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