Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/16315
Title: Active site binding modes of curcumin in HIV-1 protease and integrase
Authors: Opa Vajragupta
Preecha Boonchoong
Garrett M. Morris
Arthur J. Olson
Mahidol University
Ubon Rajathanee University
Scripps Research Institute
Keywords: Biochemistry, Genetics and Molecular Biology;Chemistry;Pharmacology, Toxicology and Pharmaceutics
Issue Date: 15-Jul-2005
Citation: Bioorganic and Medicinal Chemistry Letters. Vol.15, No.14 (2005), 3364-3368
Abstract: Structure models for the interaction of curcumin with HIV-1 integrase (IN) and protease (PR) were investigated using computational docking. Curcumin was found to bind preferentially in similar ways to the active sites of both IN and PR. For IN, the binding site is formed by residues Asp64, His67, Thr66, Glu92, Thr93, Asp116, Ser119, Asn120, and Lys159. Docked curcumin contacts the catalytic residues adjacent to Asp116 and Asp64, and near the divalent metal (Mg2+). In the PR docking, the curcumin structure fitted well to the active site, interacting with residues Asp25, Asp29, Asp30, Gly27′, Asp29′, and Asp30′. The results suggest that o-hydroxyl and/or keto-enol structures are important for both IN and PR inhibitory actions. The symmetrical structure of curcumin seems to play an important role for binding to the PR protein, whereas the keto-enol and only one side of the terminal o-hydroxyl showed tight binding to the IN active site. © 2005 Elsevier Ltd. All rights reserved.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=20644442241&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/16315
ISSN: 0960894X
Appears in Collections:Scopus 2001-2005

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.