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Chitin binding motif

Fig. 18 CG15920 gene sequence and primary structure. The consensus repeat sequences are also represented. The highlighted regions correspond to the signal sequence, R R chitin-binding domain, and the elastomeric domains containing repeat motifs A and B. Reproduced from [182, 188] with permission from Elsevier, copyright Elsevier 2001, 2010... Fig. 18 CG15920 gene sequence and primary structure. The consensus repeat sequences are also represented. The highlighted regions correspond to the signal sequence, R R chitin-binding domain, and the elastomeric domains containing repeat motifs A and B. Reproduced from [182, 188] with permission from Elsevier, copyright Elsevier 2001, 2010...
The arsenal of plant defense peptides contains members capable of binding carbohydrate residues, namely /31-4 linked A -acetyl glucosamine residues that form the biopolymer chitin. The actual mode of action remains unclear. Antifungal and antimicrobial activity has been shown in vitro. For example Ac-AMP2 is a small disulfide-rich chitin-binding peptide isolated from the seeds of Amaranthus caudatus with antimicrobial activity. It differs from Ac-AMP 1 by one additional arginine residue at the C-terminus. The structure was determined by NMR and contains a cystine knot motif. Ac-AMP2 displays a so-called hevein domain partly... [Pg.277]

T. Suetake, S. Tsuda, S. Kawabata, K. Miura, S. Iwanaga, K. Hikichi, K. Nitta, and K. Kawano, Chitin-binding proteins in invertebrates and plants comprise a common chitin-bind-ing structural motif, J. Biol. Chem., 275 (2000) 17929-17932. [Pg.354]


See other pages where Chitin binding motif is mentioned: [Pg.306]    [Pg.306]    [Pg.97]    [Pg.230]    [Pg.320]    [Pg.305]    [Pg.397]    [Pg.381]    [Pg.894]   
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