Rapid screening for HIV-1 protease inhibitor leads through X-ray diffraction

Pillai, B. ; Kannan, K. K. ; Bhat, S. V. ; Hosur, M. V. (2004) Rapid screening for HIV-1 protease inhibitor leads through X-ray diffraction Acta Crystallographica Section D: Biological Crystallography, 60 (3). pp. 594-596. ISSN 0907-4449

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Official URL: http://scripts.iucr.org/cgi-bin/paper?sx5009

Related URL: http://dx.doi.org/10.1107/S0907444903029676

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.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:HIV-1 Protease Inhibitors; AIDS Therapy
ID Code:19040
Deposited On:25 Nov 2010 14:33
Last Modified:03 Jun 2011 08:31

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