Title : Molecular dynamics study of prolyl oligopeptidase with inhibitor in binding cavity.

Pub. Date : 2009 Oct

PMID : 20024801






9 Functional Relationships(s)
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1 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
2 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
3 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
4 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
5 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
6 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
7 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
8 We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens
9 We performed 100 ns of simulation with the hemiacetal bond, through which the ZPP is bound to the POP, removed in order to better investigate the binding cavity environment. N-benzyloxycarbonylprolylprolinal prolyl endopeptidase Homo sapiens