2L37
3D solution structure of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrical)
Summary for 2L37
| Entry DOI | 10.2210/pdb2l37/pdb |
| Descriptor | Ribosome-inactivating protein luffin P1 (1 entity in total) |
| Functional Keywords | hydrolase |
| Biological source | Luffa aegyptiaca (loofa) |
| Total number of polymer chains | 1 |
| Total formula weight | 5243.93 |
| Authors | Ng, Y.M.,Yang, Y.,Sze, K.H.,Zhang, X.,Zheng, Y.T.,Shaw, P.C. (deposition date: 2010-09-08, release date: 2011-01-19, Last modification date: 2024-10-30) |
| Primary citation | Ng, Y.M.,Yang, Y.,Sze, K.H.,Zhang, X.,Zheng, Y.T.,Shaw, P.C. Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrical). J.Struct.Biol., 2010 Cited by PubMed Abstract: 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. PubMed: 21195767DOI: 10.1016/j.jsb.2010.12.007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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