Unknown

Dataset Information

0

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


ABSTRACT: 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].

SUBMITTER: Palese LL 

PROVIDER: S-EPMC5671413 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Palese Luigi Leonardo LL  

Data in brief 20171006


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]. ...[more]

Similar Datasets

| S-EPMC2705922 | biostudies-literature
| S-EPMC4306386 | biostudies-literature
| S-EPMC2810526 | biostudies-literature
| S-EPMC3210109 | biostudies-literature
| S-EPMC4160752 | biostudies-literature
| S-EPMC3205944 | biostudies-literature
| S-EPMC4493826 | biostudies-literature
| S-EPMC5988488 | biostudies-literature
| S-EPMC3107050 | biostudies-literature
| S-EPMC1088301 | biostudies-literature