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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
Saporin is a ribosome-inactivating protein (RIP); alone, saporin does not selectively inactive ribosomes but rather conjugate with other molecules like peptides [3]. Saponaria officinalis is the plant from which saporin is extracted [4]. Type I and type II RIPS exist. Of these types, saporin is a type I. Ribosome inactivating proteins catalyze a cleavages N-glycosidic bond that is formed between the ribosome and adenine [5]. This adenine has the role of binding EF-1 and EF-2 to a ribosome [5]. EF stands for elongation factor. Since adenine no longer has a bond to the ribosome, the elongation step in translation cannot occur because the elongation factors cannot bind to just the ribosome. The specific elongation factor that is inhibited is elongation factor 2, which causes irreversible damage and disallows protein synthesis [4].
Disease
Relevance
Structural highlights
Type 1 RIPS are monomeric, meaning they have one part [6]. Saporin-S6 at maturity is 256 amino acids long [4]. While saporin consists of different residues and molecules, there is only one Chain A in it, and thus is monomeric. Chain A is a polypeptide weighing 30 KDa [7]. This chain consists of beta-sheets and alpha-helixes. The β-sheets make up the N-terminal domain, while the 𝛼-helix portion is the C-terminal domain [5]. In the figure of Chain A, the 𝛼-helices are spiral-shaped strands, while the β-sheets are more of a flat strand.
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- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:https://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ Bolshakov AP, Stepanichev MY, Dobryakova YV, Spivak YS, Markevich VA. Saporin from Saponaria officinalis as a Tool for Experimental Research, Modeling, and Therapy in Neuroscience. Toxins (Basel). 2020 Aug 25;12(9). pii: toxins12090546. doi:, 10.3390/toxins12090546. PMID:32854372 doi:https://dx.doi.org/10.3390/toxins12090546
- ↑ 4.0 4.1 4.2 Polito L, Bortolotti M, Mercatelli D, Battelli MG, Bolognesi A. Saporin-S6: a useful tool in cancer therapy. Toxins (Basel). 2013 Oct 7;5(10):1698-722. doi: 10.3390/toxins5101698. PMID:24105401 doi:https://dx.doi.org/10.3390/toxins5101698
- ↑ 5.0 5.1 5.2 doi: https://dx.doi.org/10.1016/s0014-5793(00)01325-9
- ↑ Fabbrini MS, Katayama M, Nakase I, Vago R. Plant Ribosome-Inactivating Proteins: Progesses, Challenges and Biotechnological Applications (and a Few Digressions). Toxins (Basel). 2017 Oct 12;9(10). pii: toxins9100314. doi:, 10.3390/toxins9100314. PMID:29023422 doi:https://dx.doi.org/10.3390/toxins9100314
- ↑ Zhang GN, Gupta P, Wang M, Barbuti AM, Ashby CR Jr, Zhang YK, Zeng L, Xu Q, Fan YF, Chen ZS. Lipid-Saporin Nanoparticles for the Intracellular Delivery of Cytotoxic Protein to Overcome ABC Transporter-Mediated Multidrug Resistance In Vitro and In Vivo. Cancers (Basel). 2020 Feb 21;12(2). pii: cancers12020498. doi:, 10.3390/cancers12020498. PMID:32098067 doi:https://dx.doi.org/10.3390/cancers12020498
