Inhibition of HIV-1 proteinase by metal ions

Woon T.C., Brinkworth R.I. and Fairlie D.P. (1992) Inhibition of HIV-1 proteinase by metal ions. International Journal of Biochemistry, 24 6: 911-914. doi:10.1016/0020-711X(92)90096-J


Author Woon T.C.
Brinkworth R.I.
Fairlie D.P.
Title Inhibition of HIV-1 proteinase by metal ions
Journal name International Journal of Biochemistry   Check publisher's open access policy
ISSN 0020-711X
Publication date 1992
Sub-type Article (original research)
DOI 10.1016/0020-711X(92)90096-J
Volume 24
Issue 6
Start page 911
End page 914
Total pages 4
Subject 1303 Specialist Studies in Education
Abstract 1. 1. Certain metal ions have been identified as inhibitors (IC50 1-20 μM) of the aspartic proteinase of Human Immunodeficiency Virus Type 1 (HIV-PR). 2. 2. By contrast most simple metal ions do not inhibit this enzyme. 3. 3. Those that did inhibit have in common a high charge/size ratio or "hard" acidic nature, preferring to combine covalently with oxygen donor ligands. 4. 4. Some evidence from independent X-ray crystal structure determinations suggests that the metalloinhibitors identified here may bind in the active site of the enzyme via coordination to the carboxylate side chains of the essential active site residues Asp 25 and 125. 5. 5. Although the measured inhibition is only μM, very few enzyme-inhibitor interactions can be taking place and so more complex metalloinhibitors with ligands that can also bind to peptide side chains of the enzyme might be significantly more potent inhibitors of HIV-PR and of viral replication.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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Created: Tue, 28 Jun 2016, 06:14:59 EST by System User