Record Details

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

DSpace at IIT Bombay

View Archive Info
 
 
Field Value
 
Title Rapid screening for HIV-1 protease inhibitor leads through X-ray diffraction
 
Creator PILLAI, B
KANNAN, KK
BHAT, SV
HOSUR, MV
 
Subject 3-dimensional structure
aspartyl protease
crystal-structure
design
crystallography
resolution
enzyme
 
Description 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.
 
Publisher BLACKWELL MUNKSGAARD
 
Date 2011-07-19T02:28:59Z
2011-12-26T12:50:57Z
2011-12-27T05:37:12Z
2011-07-19T02:28:59Z
2011-12-26T12:50:57Z
2011-12-27T05:37:12Z
2004
 
Type Article
 
Identifier ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 60(), 594-596
0907-4449
http://dx.doi.org/10.1107/S0907444903029676
http://dspace.library.iitb.ac.in/xmlui/handle/10054/5145
http://hdl.handle.net/10054/5145
 
Language en