Analysis of the conformations of the HIV-1 protease from a large crystallographic data set

The HIV-1 protease performs essential roles in viral maturation by processing specific cleavage sites in the Gag and Gag-Pol precursor polyproteins to release their mature forms. Here the analysis of a large HIV-1 protease data set (containing 552 dimer structures) are reported. These data are relat...

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Autor principal: Palese, Luigi Leonardo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Proteomics and Biochemistry   
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5671413/
https://www.ncbi.nlm.nih.gov/pubmed/29124093
http://dx.doi.org/10.1016/j.dib.2017.09.076
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author Palese, Luigi Leonardo
author_facet Palese, Luigi Leonardo
author_sort Palese, Luigi Leonardo
collection PubMed
description The HIV-1 protease performs essential roles in viral maturation by processing specific cleavage sites in the Gag and Gag-Pol precursor polyproteins to release their mature forms. Here the analysis of a large HIV-1 protease data set (containing 552 dimer structures) are reported. These data are related to article entitled “Conformations of the HIV-1 protease: a crystal structure data set analysis” (Palese, 2017) [1].
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spelling pubmed-56714132017-11-09 Analysis of the conformations of the HIV-1 protease from a large crystallographic data set Palese, Luigi Leonardo Data Brief Proteomics and Biochemistry    The HIV-1 protease performs essential roles in viral maturation by processing specific cleavage sites in the Gag and Gag-Pol precursor polyproteins to release their mature forms. Here the analysis of a large HIV-1 protease data set (containing 552 dimer structures) are reported. These data are related to article entitled “Conformations of the HIV-1 protease: a crystal structure data set analysis” (Palese, 2017) [1]. Elsevier 2017-10-06 /pmc/articles/PMC5671413/ /pubmed/29124093 http://dx.doi.org/10.1016/j.dib.2017.09.076 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Proteomics and Biochemistry   
Palese, Luigi Leonardo
Analysis of the conformations of the HIV-1 protease from a large crystallographic data set
title Analysis of the conformations of the HIV-1 protease from a large crystallographic data set
title_full Analysis of the conformations of the HIV-1 protease from a large crystallographic data set
title_fullStr Analysis of the conformations of the HIV-1 protease from a large crystallographic data set
title_full_unstemmed Analysis of the conformations of the HIV-1 protease from a large crystallographic data set
title_short Analysis of the conformations of the HIV-1 protease from a large crystallographic data set
title_sort analysis of the conformations of the hiv-1 protease from a large crystallographic data set
topic Proteomics and Biochemistry   
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5671413/
https://www.ncbi.nlm.nih.gov/pubmed/29124093
http://dx.doi.org/10.1016/j.dib.2017.09.076
work_keys_str_mv AT paleseluigileonardo analysisoftheconformationsofthehiv1proteasefromalargecrystallographicdataset

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