Saporin: Difference between revisions
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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 == | ||
