Literature DB >> 2645523

Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1.

M A Navia1, P M Fitzgerald, B M McKeever, C T Leu, J C Heimbach, W K Herber, I S Sigal, P L Darke, J P Springer.   

Abstract

The crystal structure of the protease of the human immunodeficiency virus type (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 A resolution. Large regions of the protease dimer, including the active site, have structural homology to the family of microbial aspartyl proteases. The structure suggests a mechanism for the autoproteolytic release of protease and a role in the control of virus maturation.

Entities:  

Mesh：

Substances：

Year:  1989        PMID： 2645523     DOI： 10.1038/337615a0

Source DB:  PubMed          Journal:  Nature        ISSN： 0028-0836            Impact factor:   49.962


  160 in total

1.  Point mutations and sequence variability in proteins: redistributions of preexisting populations.

Authors:  N Sinha; R Nussinov
Journal:  Proc Natl Acad Sci U S A       Date:  2001-03-13       Impact factor: 11.205

2.  The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.

Authors:  Steven C Pettit; Sergei Gulnik; Lori Everitt; Andrew H Kaplan
Journal:  J Virol       Date:  2003-01       Impact factor: 5.103

3.  The ins and outs of presenilin 1 membrane topology.

Authors:  Jinoh Kim; Randy Schekman
Journal:  Proc Natl Acad Sci U S A       Date:  2004-01-19       Impact factor: 11.205

Review 4.  Antiretroviral therapy: strategies beyond single-agent reverse transcriptase inhibition.

Authors:  K J Connolly; S M Hammer
Journal:  Antimicrob Agents Chemother       Date:  1992-03       Impact factor: 5.191

5.  Production of cytotoxic proteins in Escherichia coli: a fermentation process for producing enzymatically active HIV-1 protease.

Authors:  W K Herber; F J Bailey; C E Carty; J C Heimbach; R Z Maigetter
Journal:  Appl Microbiol Biotechnol       Date:  1991-11       Impact factor: 4.813

6.  Protein-ligand binding free energy estimation using molecular mechanics and continuum electrostatics. Application to HIV-1 protease inhibitors.

Authors:  V Zoete; O Michielin; M Karplus
Journal:  J Comput Aided Mol Des       Date:  2003-12       Impact factor: 3.686

7.  Celebrating structural biology.

Authors: 
Journal:  Nat Struct Mol Biol       Date:  2011-12-05       Impact factor: 15.369

8.  Investigation on the mechanism for the binding and drug resistance of wild type and mutations of G86 residue in HIV-1 protease complexed with Darunavir by molecular dynamic simulation and free energy calculation.

Authors:  Dan Li; Ying Zhang; Run-Ning Zhao; Song Fan; Ju-Guang Han
Journal:  J Mol Model       Date:  2014-02-14       Impact factor: 1.810

9.  Correlation between the predicted and the observed biological activity of the symmetric and nonsymmetric cyclic urea derivatives used as HIV-1 protease inhibitors. A 3D-QSAR-CoMFA method for new antiviral drug design.

Authors:  Speranta Avram; I Svab; C Bologa; Maria-Luiza Flonta
Journal:  J Cell Mol Med       Date:  2003 Jul-Sep       Impact factor: 5.310

10.  Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation.

Authors:  L M Babé; J Rosé; C S Craik
Journal:  Proc Natl Acad Sci U S A       Date:  1995-10-24       Impact factor: 11.205
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.