Jang_2010_J.Comput.Aided.Mol.Des_24_213

Reference

Title : Docking study of the precursor peptide of mastoparan onto its putative processing enzyme, dipeptidyl peptidase IV: a revisit to molecular ticketing - Jang_2010_J.Comput.Aided.Mol.Des_24_213
Author(s) : Jang S , Chung TY , Shin J , Lin KL , Tzen JT , Li FY
Ref : J Comput Aided Mol Des , 24 :213 , 2010
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.

PubMedSearch : Jang_2010_J.Comput.Aided.Mol.Des_24_213
PubMedID: 20306218

Related information

Citations formats

Jang S, Chung TY, Shin J, Lin KL, Tzen JT, Li FY (2010)
Docking study of the precursor peptide of mastoparan onto its putative processing enzyme, dipeptidyl peptidase IV: a revisit to molecular ticketing
J Comput Aided Mol Des 24 :213

Jang S, Chung TY, Shin J, Lin KL, Tzen JT, Li FY (2010)
J Comput Aided Mol Des 24 :213