Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/xmlui/handle/10054/5145
Title: Rapid screening for HIV-1 protease inhibitor leads through X-ray diffraction
Authors: PILLAI, B
KANNAN, KK
BHAT, SV
HOSUR, MV
Keywords: 3-Dimensional Structure
Aspartyl Protease
Crystal-Structure
Design
Crystallography
Resolution
Enzyme
Issue Date: 2004
Publisher: BLACKWELL MUNKSGAARD
Citation: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 60(), 594-596
Abstract: Knowledge of the three-dimensional structures of HIV-1 protease and of its complexes with various inhibitors has played a key role in development of drugs against AIDS. Hexagonal crystals of unliganded tethered HIV-1 protease in which the enzyme conformation is identical to its ligand-bound state can be used in combination with the soaking method in order to identify potential inhibitor leads via X-ray diffraction. The advantages of the soaking method are the generality of application and the rapidity of structure determination for iterative structure-based drug design. Structures of two ligand complexes with HIV-1 protease determined using this method are shown to be very similar to the structures obtained earlier via co-crystallization.
URI: http://dx.doi.org/10.1107/S0907444903029676
http://dspace.library.iitb.ac.in/xmlui/handle/10054/5145
http://hdl.handle.net/10054/5145
ISSN: 0907-4449
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