Title : Prediction of interaction mode between a typical ACE inhibitor and MMP-9 active site.

Pub. Date : 2007 Mar 23

PMID : 17275782






3 Functional Relationships(s)
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1 To characterize the inhibitory specificity of angiotensin converting enzyme (ACE) inhibitors for matrix metalloproteinase 9 (MMP-9) activity, molecular modeling of these complex was performed referring the recent X-ray structure analyses using lisinopril as an ACE inhibitor. Lisinopril matrix metallopeptidase 9 Homo sapiens
2 To characterize the inhibitory specificity of angiotensin converting enzyme (ACE) inhibitors for matrix metalloproteinase 9 (MMP-9) activity, molecular modeling of these complex was performed referring the recent X-ray structure analyses using lisinopril as an ACE inhibitor. Lisinopril matrix metallopeptidase 9 Homo sapiens
3 Lisinopril was effectively stabilized by specific hydrogen bonds and hydrophobic interactions in the active site of MMP-9, and its hydrophobic group appeared to interact preferentially with the S1 site compared with the S1" site. Lisinopril matrix metallopeptidase 9 Homo sapiens