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Expression, purification and preliminary X‐ray crystallographic studies of the human immunodeficiency virus 1 subtype C protease

Expression, purification and preliminary X‐ray crystallographic studies of the human... Crystals of the human immunodeficiency virus 1 (HIV‐1) subtype C protease (PR) complexed with the clinically used inhibitors indinavir (IDV) and nelfinavir (NFV) have been grown in the monoclinic space group P21, with mean unit‐cell parameters a = 46.7 (±0.1), b = 59.8 (±0.3), c = 87.0 (±0.4) Å, β = 95.2 (±0.5)°. The crystals of both complexes have been shown to diffract X‐rays to 2.3 Å resolution. The diffraction data for the subtype C PR complexes with IDV and NFV were subsequently processed and reduced, with overall Rsym values of 8.4 and 11.4%, respectively. Based on the unit‐cell volumes, molecular‐replacement results and packing considerations, there are two protease homodimers per crystallographic asymmetric unit in each of the complexes. The data were initially phased using a model based on the crystal structure of HIV‐1 subtype B PR; the structures have been determined and further refinement and analysis are in progress. These structures and subsequent studies with other inhibitors will greatly aid in correlating the amino‐acid variation between the different HIV PRs and understanding their differential sensitivity and resistance to current drug therapy. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Expression, purification and preliminary X‐ray crystallographic studies of the human immunodeficiency virus 1 subtype C protease

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References (55)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430910701161X
pmid
17401206
Publisher site
See Article on Publisher Site

Abstract

Crystals of the human immunodeficiency virus 1 (HIV‐1) subtype C protease (PR) complexed with the clinically used inhibitors indinavir (IDV) and nelfinavir (NFV) have been grown in the monoclinic space group P21, with mean unit‐cell parameters a = 46.7 (±0.1), b = 59.8 (±0.3), c = 87.0 (±0.4) Å, β = 95.2 (±0.5)°. The crystals of both complexes have been shown to diffract X‐rays to 2.3 Å resolution. The diffraction data for the subtype C PR complexes with IDV and NFV were subsequently processed and reduced, with overall Rsym values of 8.4 and 11.4%, respectively. Based on the unit‐cell volumes, molecular‐replacement results and packing considerations, there are two protease homodimers per crystallographic asymmetric unit in each of the complexes. The data were initially phased using a model based on the crystal structure of HIV‐1 subtype B PR; the structures have been determined and further refinement and analysis are in progress. These structures and subsequent studies with other inhibitors will greatly aid in correlating the amino‐acid variation between the different HIV PRs and understanding their differential sensitivity and resistance to current drug therapy.

Journal

Acta Crystallographica Section FWiley

Published: Apr 1, 2007

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