Saporin
From Proteopedia
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==Your Heading Here (maybe something like 'Structure')== | ==Your Heading Here (maybe something like 'Structure')== | ||
| - | <StructureSection load=' | + | <StructureSection load='1QI7' size='340' side='right' caption='Caption for this structure' scene=''> |
This is a default text for your page '''Saporin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page '''Saporin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
| - | Saporin | + | Saporin is a ribosome-inactivating protein (RIP); alone, saporin does not selectively inactive ribosomes but rather conjugate with other molecules like peptides <ref name="basel">DOI: |
| + | 10.3390/toxins12090546</ref>. Saponaria officinalis is the plant from which saporin is extracted <ref name="ncbi">DOI: 10.3390/toxins5101698</ref>. 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 <ref name="rcsb">DOI: 10.1016/s0014-5793(00)01325-9</ref>. This adenine has the role of binding EF-1 and EF-2 to a ribosome <ref name="rcsb" />. | ||
== Disease == | == Disease == | ||
Revision as of 17:44, 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
- ↑ 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 doi: https://dx.doi.org/10.1016/s0014-5793(00)01325-9
