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

Luigi Leonardo Palese

doi:10.1016/j.dib.2017.09.076

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

Data Brief. 2017 Oct 6:15:696-700. doi: 10.1016/j.dib.2017.09.076. eCollection 2017 Dec.

Author

Luigi Leonardo Palese¹

Affiliation

¹ University of Bari "Aldo Moro", Department of Basic Medical Sciences, Neurosciences and Sense Organs (SMBNOS), Bari 70124, Italy.

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].