Tachyplesin: Difference between revisions
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== Relevance == | == Relevance == | ||
== Mode of action == | == Mode of action == | ||
TPI can bind to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity to LPS gained by interaction between cationic residues of TPI with phosphate group and sachharides of LPS. Furthermore, interaction between hydrophobic residues of TPI with acyl chains of LPS strengthens the TPI/LPS interaction. | TPI can bind to LPS and also has ability to permeabilize the cell membrane of pathogens. Docking model suggests strong affinity to LPS gained by interaction between cationic residues of TPI with phosphate group and sachharides of LPS. Furthermore, interaction between hydrophobic residues of TPI with acyl chains of LPS strengthens the TPI/LPS interaction. The binding of TPI to LPS neutralizes LPS, which is widely considered as endotoxin. In addition to LPS binding, footpriting analysis has revealed the binding of TPI to DNA by interacting specifically in minor groove of DNA duplex. The interaction between TPI and DNA is contributed by secondary structure of the peptide which contains an antiparallel beta-sheet constrained by two disulfide bridges and connected by beta-turn. | ||
== Function == | == Function == | ||
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. | ||
