Tachyplesin: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 10: | Line 10: | ||
[[Image:scheme.jpg|150px|left|thumb|<b>Figure 1: Simplefied model of Tachyplesin I.</b>]] | [[Image:scheme.jpg|150px|left|thumb|<b>Figure 1: Simplefied model of Tachyplesin I.</b>]] | ||
The sequence adapts antiparallel β-sheet (hairpin) conformation in solution stabilized by two cross-strand <scene name='67/671725/Disulfide_bonds/1'> disulfide bonds </scene> between Cys³-Cys¹⁶ and Cys⁷-Cys¹²<ref name=Nakamura>Nakamura, Takanori, et al. "Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure." Journal of Biological Chemistry 263.32 (1988): 16709-16713</ref>, and its [http://en.wikipedia.org/wiki/Protein_primary_structure C-terminus is amidated].<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref>. Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. | |||
The β-hairpin structure is well characterized by a β-turn for the centrally located residues Tyr-Arg-Gly-Ile.<ref name=Saravanan>PMID:22464970</ref> | |||
| Line 15: | Line 19: | ||
