Structural highlights
Function
RIP1_LUFAE Inhibits protein synthesis in animal cells.[1]
Publication Abstract from PubMed
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.
Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica).,Ng YM, Yang Y, Sze KH, Zhang X, Zheng YT, Shaw PC J Struct Biol. 2010 Dec 31. PMID:21195767[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li F, Yang XX, Xia HC, Zeng R, Hu WG, Li Z, Zhang ZC. Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica. Peptides. 2003 Jun;24(6):799-805. PMID:12948831
- ↑ Ng YM, Yang Y, Sze KH, Zhang X, Zheng YT, Shaw PC. Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica). J Struct Biol. 2010 Dec 31. PMID:21195767 doi:10.1016/j.jsb.2010.12.007
