Saporin

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<scene name='91/910029/Active_site_tyr_120/1'>Text To Be Displayed</scene><scene name='91/910029/Active_site/1'>Text To Be Displayed</scene>==Your Heading Here (maybe something like 'Structure')==
 
<StructureSection load='1qi7' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='1qi7' size='340' side='right' caption='Caption for this structure' scene=''>
== Function ==
== Function ==
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Type 1 RIPS are monomeric, meaning they have one part <ref name="fab">DOI: 10.3390/toxins9100314</ref>. Saporin-S6 at maturity is 256 amino acids long <ref name="ncbi" />. 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 <ref name="nano">DOI: 10.3390/cancers12020498</ref>. 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 <ref name="rcsb" />. In the figure of Chain A, the 𝛼-helices are spiral-shaped strands, while the β-sheets are more of a flat strand.
Type 1 RIPS are monomeric, meaning they have one part <ref name="fab">DOI: 10.3390/toxins9100314</ref>. Saporin-S6 at maturity is 256 amino acids long <ref name="ncbi" />. 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 <ref name="nano">DOI: 10.3390/cancers12020498</ref>. 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 <ref name="rcsb" />. 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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There is an <scene name='91/910029/Active_site/1'>active site</scene> within this chain that consists of five residues. These residues are <scene name='91/910569/Active_site_tyr/1'>Tyr⁷²</scene>, <scene name='91/910029/Active_site_tyr_120/1'>Tyr¹²⁰</scene>, <scene name='91/910029/Active_site_glu_176/1'>Glu¹⁷⁶</scene>, <scene name='91/910029/Active_site_arg_179/1'>Arg¹⁷⁹</scene>, and Trp²⁰⁸ <ref name="ncbi">DOI: 10.3390/toxins5101698</ref>. Other RIPs also have these same residues in their active sites. The saporin active has Glu¹⁷⁶, Arg¹⁷⁹, and Trp²⁰⁸ in the exact same position as the other ribosome-inactivating proteins. There is a difference in Tyr⁷², which has different side-chain conformations in RIPs and thus is not the same in saporin and other RIPs. This Tyr⁷² is the residue that interacts with the adenine in the cleavage of adenine and the ribosome <ref name="rcsb" />.
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There is an <scene name='91/910029/Active_site/1'>active site</scene> within this chain that consists of five residues. These residues are <scene name='91/910569/Active_site_tyr/1'>Tyr⁷²</scene>, <scene name='91/910029/Active_site_tyr_120/1'>Tyr¹²⁰</scene>, <scene name='91/910029/Active_site_glu_176/1'>Glu¹⁷⁶</scene>, <scene name='91/910029/Active_site_arg_179/3'>Arg¹⁷⁹</scene>, and <scene name='91/910029/Active_site208/2'>Trp²⁰⁸</scene> <ref name="ncbi">DOI: 10.3390/toxins5101698</ref>. Other RIPs also have these same residues in their active sites. The saporin active has Glu¹⁷⁶, Arg¹⁷⁹, and Trp²⁰⁸ in the exact same position as the other ribosome-inactivating proteins. There is a difference in Tyr⁷², which has different side-chain conformations in RIPs and thus is not the same in saporin and other RIPs. This Tyr⁷² is the residue that interacts with the adenine in the cleavage of adenine and the ribosome <ref name="rcsb" />.
Saporin can also be complexed with other inhibitors. One of these is cyclic tetranucleotide inhibitor in <scene name='91/910569/Complex_of_saporin_with_tetra/1'>complex with saporin-L1</scene>. This can be used because the cyclic tetranucleotide can take the place of the recognition loop for saporin of 28S rRNA <ref name="pnas">DOI: 0.1073/pnas.0911606106</ref>. It is also interesting to note that Ricin can also be complex with other inhibitors like saporin. Saporin is a homologue of Ricin A-Chain which means they are similar in structure <ref name="pnas" />. This ability also allows for saporin-S6 to be conjugated with specific targeting proteins, and thus the saporin-S6 is able to be delivered to the cell. This happens due to the antibodies and is referred to as an immunotoxin <ref name="ncbi" />. The antibodies are recognized by the cell, and the cell binds them. Since the saporin-S6 is in complex with the antibody, it is also taken to the cell. Some other carries can also be used, such as growth factors, antigens, and growth hormones <ref name="ncbi" />.
Saporin can also be complexed with other inhibitors. One of these is cyclic tetranucleotide inhibitor in <scene name='91/910569/Complex_of_saporin_with_tetra/1'>complex with saporin-L1</scene>. This can be used because the cyclic tetranucleotide can take the place of the recognition loop for saporin of 28S rRNA <ref name="pnas">DOI: 0.1073/pnas.0911606106</ref>. It is also interesting to note that Ricin can also be complex with other inhibitors like saporin. Saporin is a homologue of Ricin A-Chain which means they are similar in structure <ref name="pnas" />. This ability also allows for saporin-S6 to be conjugated with specific targeting proteins, and thus the saporin-S6 is able to be delivered to the cell. This happens due to the antibodies and is referred to as an immunotoxin <ref name="ncbi" />. The antibodies are recognized by the cell, and the cell binds them. Since the saporin-S6 is in complex with the antibody, it is also taken to the cell. Some other carries can also be used, such as growth factors, antigens, and growth hormones <ref name="ncbi" />.

Current revision

Caption for this structure

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References

  1. ↑ 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:http://dx.doi.org/10.3390/toxins12090546
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 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:http://dx.doi.org/10.3390/toxins5101698
  3. ↑ 3.0 3.1 3.2 3.3 doi: https://dx.doi.org/10.1016/s0014-5793(00)01325-9
  4. ↑ 4.0 4.1 4.2 4.3 4.4 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:http://dx.doi.org/10.3390/toxins9100314
  5. ↑ 5.0 5.1 5.2 5.3 5.4 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:http://dx.doi.org/10.3390/cancers12020498
  6. ↑ 6.0 6.1 doi: https://dx.doi.org/0.1073/pnas.0911606106
  7. ↑ 7.0 7.1 7.2 7.3 Zuppone S, Assalini C, Minici C, Bertagnoli S, Branduardi P, Degano M, Fabbrini MS, Montorsi F, Salonia A, Vago R. The anti-tumoral potential of the saporin-based uPAR-targeting chimera ATF-SAP. Sci Rep. 2020 Feb 13;10(1):2521. doi: 10.1038/s41598-020-59313-8. PMID:32054892 doi:http://dx.doi.org/10.1038/s41598-020-59313-8

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