Tachyplesin

Headline text

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Tachyplesin I (TP I) (TPI) is an antimicrobial polypeptide originally detected in Japanese Horse Shoe Crab. It shows high affinity for lipopolysaccharides (LPS) of gram-negative bacteria, thus neutralizing its effects. It has also been reported to inhibit the growth of gram positive bacteria, fungui and viruses. Structural highlights The aminoacid sequence of the TPI is H-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-NH₂ with disulfide bonds between Cys³ and Cys¹⁶/Cys⁷ and Cys¹². Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. Since linear tachyplesin analogues do not show preferential affinity for LPS, the hairpin properties of the peptide seems to be important for recognition of lipopolysaccharides and its biological activities. TPI undergoes confirmation change in presence of LPS. The backbone of the polypeptide becomes more rigid and twisted in presence of LPS, making it more stable. Function This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

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Shulamit Idzikowski, Janak Raj Joshi, Michal Harel, Angel Herraez, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman