2l37

3D solution structure of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrical)

spinqualitylabelsall models 2l37 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l37 is a 1 chain structure with sequence from Luffa aegyptiaca. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RIP1_LUFAE Inhibits protein synthesis in animal cells. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosome inactivating protein 3D structures

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