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- W2019521836 abstract "Abstract Vigna radiata plant defensin 1 (VrD1) is the first reported plant defensin exhibiting insecticidal activity. We report herein the nuclear magnetic resonance solution structure of VrD1 and the implication on its insecticidal activity. The root‐mean‐square deviation values are 0.51 ± 0.35 and 1.23 ± 0.29 Å for backbone and all heavy atoms, respectively. The VrD1 structure comprises a triple‐stranded antiparallel β‐sheet, an α‐helix, and a 3 10 helix stabilized by four disulfide bonds, forming a typical cysteine‐stabilized αβ motif. Among plant defensins of known structure, VrD1 is the first to contain a 3 10 helix. Glu 26 is highly conserved among defensins; VrD1 contains an arginine at this position, which may induce a shift in the orientation of Trp 10 , thereby promoting the formation of this 3 10 helix. Moreover, VrD1 inhibits Tenebrio molitor α‐amylase. α‐Amylase has an essential role in the digestion of plant starch in the insect gut, and expression of the common bean α‐amylase inhibitor 1 in transgenic pea imparts complete resistance against bruchids. These results imply that VrD1 insecticidal activity has its basis in the inhibition of a polysaccharide hydrolase. Sequence and structural comparisons between two groups of plant defensins having different specificity toward insect α‐amylase reveal that the loop between β2 and β3 is the probable binding site for the α‐amylase. Computational docking experiments were used to study VrD1–α‐amylase interactions, and these results provide information that may be used to improve the insecticidal activity of VrD1. Proteins 2006. © 2006 Wiley‐Liss, Inc." @default.
- W2019521836 created "2016-06-24" @default.
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- W2019521836 date "2006-03-16" @default.
- W2019521836 modified "2023-10-16" @default.
- W2019521836 title "Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids" @default.
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- W2019521836 doi "https://doi.org/10.1002/prot.20962" @default.
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