5K79

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

5K79 の概要

• エントリーDOI: 10.2210/pdb5k79/pdb
• 分子名称: Cyanovirin-N domain protein, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: sugar binding lectin, hiv-inactivating, antiviral protein, oligosaccharide
• 由来する生物種: Cyanothece sp. (strain PCC 7424)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24146.15

構造登録者

Matei, E.,Basu, R.,Furey, W.,Shi, J.,Calnan, C.,Aiken, C.,Gronenborn, A.M. (登録日: 2016-05-25, 公開日: 2016-07-20, 最終更新日: 2023-09-27)

主引用文献

Matei, 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

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

実験手法

X-RAY DIFFRACTION (1.6 Å)