Biology:Tachystatin

From HandWiki
Tachystatin_A
PDB 1cix EBI.jpg
Three-dimensional structure of antimicrobial peptide tachystatin A. PDB entry 1cix[1]
Identifiers
SymbolTachystatin_A
PfamPF11406
InterProIPR022717
OPM superfamily112
OPM protein2dcv
Tachystatin_B
Identifiers
SymbolTachystatin_B
PfamPF11478
Pfam clanCL0083
InterProIPR020957

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. 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. 
  2. "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. 
This article incorporates text from the public domain Pfam and InterPro: IPR022717