Saporin: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 12: | Line 12: | ||
== 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. | ||
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')
| ||||||||||||
