Ribosome inactivating protein

From Proteopedia

Ribosome inactivating protein from pokeweed complex with adenine (PDB code 1qci) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Ribosome inactivating protein (RIP) is a bacterial or plant toxin which inhibits protein synthesis. RIP inactivates the ribosomal 60S subunit by N-glycosidic cleavage which results in releasing a specific adenine from 28S rRNA[1]. Type 1 RIP have a single chain, while type 2 RIP (i.e., ricin, ebulin and nigrin) have two chains. Momorcharin is a RIP isolated from several plants[2]. Trichosanthin is a RIP isolated from snake gourd[3]. Relevance RIP is being investigated as an immunotoxin for cancer treatment. Besides the anti-tumor activity of RIP, it was shown to have antiviral, antifungal, insecticidal, ribonuclease and deoxyribonuclease activities. Enhanced expression of RIP in plants confers an increased resistance to virus, fungi, insects, drought and salinity. α-momorcharin has potent inhibitory effect on some cancer cells[4]. Structural highlights The [5]. Water molecules are shown as red spheres.

3D Structures of ribosome inactivating protein

Ribosome inactivating protein 3D structures

References

1. ↑ Stirpe F, Barbieri L. Ribosome-inactivating proteins up to date. FEBS Lett. 1986 Jan 20;195(1-2):1-8. PMID:3510899
2. ↑ Wang S, Zheng Y, Yan J, Zhu Z, Wu Z, Ding Y. Alpha-momorcharin: a ribosome-inactivating protein from Momordica charantia, possessing DNA cleavage properties. Protein Pept Lett. 2013 Nov;20(11):1257-63. PMID:23777339
3. ↑ Shaw PC, Lee KM, Wong KB. Recent advances in trichosanthin, a ribosome-inactivating protein with multiple pharmacological properties. Toxicon. 2005 May;45(6):683-9. PMID:15804517 doi:10.1016/j.toxicon.2004.12.024
4. ↑ Ng TB, Liu WK, Sze SF, Yeung HW. Action of alpha-momorcharin, a ribosome inactivating protein, on cultured tumor cell lines. Gen Pharmacol. 1994 Jan;25(1):75-7. PMID:8026716
5. ↑ Kurinov IV, Myers DE, Irvin JD, Uckun FM. X-ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA substrate analogs. Protein Sci. 1999 Sep;8(9):1765-72. PMID:10493577