Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)
| Autor: | Yinhua Yang, Yiu-Ming Ng, Kong-Hung Sze, Yong-Tang Zheng, Xuan Zhang, Pang-Chui Shaw |
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| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
Magnetic Resonance Spectroscopy biology Anti-HIV Agents Ribosome-inactivating protein Circular Dichroism RNA Peptide Electrophoretic Mobility Shift Assay Enzyme-Linked Immunosorbent Assay biology.organism_classification Genes env Complementation HIV Rev response element Biochemistry chemistry Structural Biology Hydrolase Seeds HIV-1 Gourd Luffa Peptides Alpha helix |
| Zdroj: | Journal of structural biology. 174(1) |
| ISSN: | 1095-8657 |
| Popis: | Luffin P1, the smallest ribosome-inactivating peptide from the seeds of Luffa cylindrica was found to have anti-HIV-1 activity in HIV-1 infected C8166 T-cell lines and be able to bind with HIV Rev Response Element. Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a helix-loop-helix motif, with the two alpha helices tightly associated by two disulfide bonds. Based on our findings, we conclude that unlike the well-studied ribosome-inactivating proteins, which exert their action through N-glycosidase activities, Luffin P1 demonstrates a novel inactivation mechanism probably through the charge complementation with viral or cellular proteins. Our work also provides a new scaffold for the design of novel inhibitors from a simple helical motif. |
| Databáze: | OpenAIRE |
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