ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007
Expression, purification and preliminary X-ray crystallographic studies of the human immunodeficiency virus 1 subtype C protease.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 8 citations in OpenAlex.
- Pulsed EPR characterization of HIV-1 protease conformational sampling and inhibitor-induced population shifts.Physical chemistry chemical physics : PCCP · 2016Article
- Structure of the unbound form of HIV-1 subtype A protease: comparison with unbound forms of proteases from other HIV subtypes.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Structural analysis of human immunodeficiency virus type 1 CRF01_AE protease in complex with the substrate p1-p6.Journal of virology · 2008Article
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5 authors at 1 institution in 1 country.
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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 P2(1), with mean unit-cell parameters a = 46.7 (+/-0.1), b = 59.8 (+/-0.3), c = 87.0 (+/-0.4) A, beta = 95.2 (+/-0.5) degrees. The crystals of both complexes have been shown to diffract X-rays to 2.3 A resolution. The diffraction data for the subtype C PR complexes with IDV and NFV were subsequently processed and reduced, with overall R(sym) 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.
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