Literature DB >> 12651121

HIV-1 protease variants from 100-fold drug resistant clinical isolates: expression, purification, and crystallization.

John F Vickrey1, Bradley C Logsdon, Gheorghe Proteasa, Sarah Palmer, Mark A Winters, Thomas C Merigan, Ladislau C Kovari.   

Abstract

High-resolution X-ray crystallographic structures of HIV-1 protease clinical variants complexed with licensed inhibitors are essential to understanding the fundamental cause of protease drug resistance. There is a need for structures of naturally evolved HIV-1 proteases from patients failing antiretroviral therapy. Here, we report the expression, purification, and crystallization of clinical isolates of HIV-1 protease that have been characterized to be more than 100 times less susceptible to US FDA approved protease inhibitors.

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Year:  2003        PMID: 12651121     DOI: 10.1016/s1046-5928(02)00650-2

Source DB:  PubMed          Journal:  Protein Expr Purif        ISSN: 1046-5928            Impact factor:   1.650


  14 in total

1.  Rational design of p53, an intrinsically unstructured protein, for the fabrication of novel molecular sensors.

Authors:  Melissa L Geddie; Taryn L O'Loughlin; Kristen K Woods; Ichiro Matsumura
Journal:  J Biol Chem       Date:  2005-08-23       Impact factor: 5.157

2.  Diversification and specialization of HIV protease function during in vitro evolution.

Authors:  Taryn L O'Loughlin; Dina N Greene; Ichiro Matsumura
Journal:  Mol Biol Evol       Date:  2006-01-19       Impact factor: 16.240

3.  HIV protease-activated molecular switches based on beta-glucuronidase and alkaline phosphatase.

Authors:  Taryn L O'Loughlin; Ichiro Matsumura
Journal:  Comb Chem High Throughput Screen       Date:  2006-05       Impact factor: 1.339

4.  Contribution of the 80s loop of HIV-1 protease to the multidrug-resistance mechanism: crystallographic study of MDR769 HIV-1 protease variants.

Authors:  Ravikiran S Yedidi; Georghe Proteasa; Jorge L Martinez; John F Vickrey; Philip D Martin; Zdzislaw Wawrzak; Zhigang Liu; Iulia A Kovari; Ladislau C Kovari
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2011-05-17

5.  Nine crystal structures determine the substrate envelope of the MDR HIV-1 protease.

Authors:  Zhigang Liu; Yong Wang; Joseph Brunzelle; Iulia A Kovari; Ladislau C Kovari
Journal:  Protein J       Date:  2011-03       Impact factor: 2.371

6.  Crystal structures of multidrug-resistant HIV-1 protease in complex with two potent anti-malarial compounds.

Authors:  Ravikiran S Yedidi; Zhigang Liu; Yong Wang; Joseph S Brunzelle; Iulia A Kovari; Patrick M Woster; Ladislau C Kovari; Deepak Gupta
Journal:  Biochem Biophys Res Commun       Date:  2012-03-24       Impact factor: 3.575

7.  The higher barrier of darunavir and tipranavir resistance for HIV-1 protease.

Authors:  Yong Wang; Zhigang Liu; Joseph S Brunzelle; Iulia A Kovari; Tamaria G Dewdney; Samuel J Reiter; Ladislau C Kovari
Journal:  Biochem Biophys Res Commun       Date:  2011-08-17       Impact factor: 3.575

8.  Subtype polymorphisms among HIV-1 protease variants confer altered flap conformations and flexibility.

Authors:  Jamie L Kear; Mandy E Blackburn; Angelo M Veloro; Ben M Dunn; Gail E Fanucci
Journal:  J Am Chem Soc       Date:  2009-10-21       Impact factor: 15.419

9.  Crystal structures of a multidrug-resistant human immunodeficiency virus type 1 protease reveal an expanded active-site cavity.

Authors:  Bradley C Logsdon; John F Vickrey; Philip Martin; Gheorghe Proteasa; Jay I Koepke; Stanley R Terlecky; Zdzislaw Wawrzak; Mark A Winters; Thomas C Merigan; Ladislau C Kovari
Journal:  J Virol       Date:  2004-03       Impact factor: 5.103

10.  A multi-drug resistant HIV-1 protease is resistant to the dimerization inhibitory activity of TLF-PafF.

Authors:  Ravikiran S Yedidi; Gheorghe Proteasa; Philip D Martin; Zhigang Liu; John F Vickrey; Iulia A Kovari; Ladislau C Kovari
Journal:  J Mol Graph Model       Date:  2014-07-04       Impact factor: 2.518

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