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Docking study of the precursor peptide of matoparan onto its putative processing enzyme, dipeptidyl peptidase IV: a revisit to molecular ticketing

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Abstract

Stepwise-cleavage process of promastoparans to reach maturity was investigated theoretically by combining ab initio folding and unbounded docking. The comparison between the structures of the promastoparans both before and after docking were examined along with the hydrogen bonding interaction pattern between the dipetidyl peptidase IV (DPPIV) and promastoparans to reveal how the endpoint of this stepwise cleavage is recognized among these promastoparans with highly resemble amino acid sequences. The current approach of folding and docking study provides structural insight on the stepwise cleavage process.

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Acknowledgments

The National Center for High-Performance Computing in Taiwan are acknowledged for providing the computational resources. SJ appreciate financial support from Korea Research Foundation grant no. C00369 (102969). FYL appreciate National Science Council, Taiwan for its financial support.

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Authors and Affiliations

  1. Department of Chemistry and Institute for Chemical Biology, Sejong University, Seoul, 143-747, Korea

    Soonmin Jang & Jungho Shin

  2. Graduate Institute of Biotechnology, National Chung Hsing University, Taichung, Taiwan

    Tse-Yu Chung & Jason T. C. Tzen

  3. Department of Chemistry, National Chung Hsing University, Taichung, Taiwan

    Kai-Lun Lin & Feng-Yin Li

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  1. Soonmin Jang
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Correspondence to Feng-Yin Li.

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Jang, S., Chung, TY., Shin, J. et al. Docking study of the precursor peptide of matoparan onto its putative processing enzyme, dipeptidyl peptidase IV: a revisit to molecular ticketing. J Comput Aided Mol Des 24, 213–224 (2010). https://doi.org/10.1007/s10822-010-9327-7

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