Biology:Tachystatin
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Revision as of 20:48, 18 August 2022 by imported>Unex (fix)
| Tachystatin_A | |||||||||
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| Identifiers | |||||||||
| Symbol | Tachystatin_A | ||||||||
| Pfam | PF11406 | ||||||||
| InterPro | IPR022717 | ||||||||
| OPM superfamily | 112 | ||||||||
| OPM protein | 2dcv | ||||||||
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| Tachystatin_B | |||||||||
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| Identifiers | |||||||||
| Symbol | Tachystatin_B | ||||||||
| Pfam | PF11478 | ||||||||
| Pfam clan | CL0083 | ||||||||
| InterPro | IPR020957 | ||||||||
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Tachystatins are antimicrobial chitin-binding peptides from Japanese horseshoe crab. Amino acid residues Tyr(14) and Arg(17) in Tachystatin B are thought to be the essential residues for chitin binding.[2] These small proteins contain a cysteine-stabilised triple-stranded beta-sheet with an inhibitor cystine knot motif and show features common to membrane-interactive peptides. Tachystatin A is thought to have an antimicrobial activity similar to defensins.[1]
References
- ↑ 1.0 1.1 "Structure of the antimicrobial peptide tachystatin A". J. Biol. Chem. 277 (26): 23651–7. June 2002. doi:10.1074/jbc.M111120200. PMID 11959852.
- ↑ "The solution structure of horseshoe crab antimicrobial peptide tachystatin B with an inhibitory cystine-knot motif". J. Pept. Sci. 13 (4): 269–79. April 2007. doi:10.1002/psc.846. PMID 17394123.
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