The structure of a novel insect Peptide explains its ca(2+) channel blocking and antifungal activities(,).

The structure of a novel insect Peptide explains its ca(2+) channel blocking and antifungal activities(,). Research Abstract Details 

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The structure of a novel insect Peptide explains its ca(2+) channel blocking and antifungal activities(,). Abstract Text:

Takahide Kouno,Mineyuki Mizuguchi,Hiromasa Tanaka,Ping Yang,Yoshihiro Mori,Hiroyuki Shinoda,Kana Unoki,Tomoyasu Aizawa,Makoto Demura,Koichi Suzuki,Keiichi Kawano,Takahide Kouno,Mineyuki Mizuguchi,Hiromasa Tanaka,Ping Yang,Yoshihiro Mori,Hiroyuki Shinoda,Kana Unoki,Tomoyasu Aizawa,Makoto Demura,Koichi Suzuki,Keiichi Kawano,

Diapause-specific peptide (DSP), derived from the leaf beetle, inhibits Ca2+ channels and has antifungal activity. DSP acts on chromaffin cells of the adrenal medulla in a fashion similar to that of omega-conotoxin GVIA, a well-known neurotoxic peptide, and blocks N-type voltage-dependent Ca2+ channels. However, the amino acid sequence of DSP has little homology with any other known Ca2+ channel blockers or antifungal peptides. In this paper, we analyzed the solution structure of DSP by using two-dimensional 1H nuclear magnetic resonance and determined the pairing of half-cystine residues forming disulfide bonds. The arrangement of the three disulfide bridges in DSP was distinct from that of other antifungal peptides and conotoxins. The overall structure of DSP is compact due in part to the three disulfide bridges and, interestingly, is very similar to those of the insect- and plant-derived antifungal peptides. On the other hand, the disulfide arrangement and the three-dimensional structure of DSP and GVIA are not similar. Nevertheless, some surface residues of DSP superimpose on the key functional residues of GVIA. This homologous distribution of hydrophobic and charged side chains may result in the functional similarity between DSP and GVIA. Thus, we propose here that the three-dimensional structure of DSP can explain its dual function as a Ca2+ channel blocker and antifungal peptide.

The structure of a novel insect Peptide explains its ca(2+) channel blocking and antifungal activities(,). Publishing Authors By Initials

T Kouno,M Mizuguchi,H Tanaka,P Yang,Y Mori,H Shinoda,K Unoki,T Aizawa,M Demura,K Suzuki,K Kawano,T Kouno,M Mizuguchi,H Tanaka,P Yang,Y Mori,H Shinoda,K Unoki,T Aizawa,M Demura,K Suzuki,K Kawano,

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The structure of a novel insect Peptide explains its ca(2+) channel blocking and antifungal activities(,). Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biochemistry

VOLUME: 46

Page Numbers: 13733-41

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 10

MONTH: 11

YEAR: 2007

The structure of a novel insect Peptide explains its ca(2+) channel blocking and antifungal activities(,). Information

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LANGUAGE: eng

NlmUniqueID: 370623

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Grant and Affiliation Information for The structure of a novel insect Peptide explains its ca(2+) channel blocking and antifungal activities(,).

AFFILIATION: Faculty of Pharmaceutical Sciences, University of Toyama, Toyama 930-0194, Faculty of Agriculture, Iwate University, Morioka 020-8550, and Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan.

Country: United States

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MEDLINETA: Biochemistry

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