Tachyplesin I as a model peptide for antiparallel beta-sheet DNA binding motif.
In this study, we present a model compound for antiparallel beta-sheet-DNA interaction. Tachyplesin I, cationic antimicrobial peptide, interacts through contacts with the minor groove. Secondary structure of tachyplesin I, antiparallel beta-sheet constrained by two disulfide bridges and connected by beta-turn, contributes significantly to its DNA binding. The present results give valuable information for design of sequence-specific DNA binding peptide based on antiparallel beta-sheet.
Yonezawa
A
A
Institute for Chemical Research, Kyoto University, Japan.
Sugiura
Y
Y
D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000737:chemistry / Q000378:metabolism*; D023181:Antimicrobial Cationic Peptides; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic; D017433:Protein Structure, Secondary
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D004268:DNA-Binding Proteins; D010456:Peptides, Cyclic; C057636:tachyplesin peptide, Tachypleus tridentatus; D004247:DNA