Saporin
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
- | 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 active site within this chain that consists of five residues. These residues are Tyr⁷², Tyr¹²⁰, Glu¹⁷⁶, Arg¹⁷⁹, 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" />. | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. |
Revision as of 16:54, 21 April 2022
Your Heading Here (maybe something like 'Structure')
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References
- ↑ 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:http://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:http://dx.doi.org/10.3390/toxins12090546
- ↑ 4.0 4.1 4.2 4.3 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
- ↑ 5.0 5.1 5.2 5.3 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:http://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:http://dx.doi.org/10.3390/cancers12020498