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Analysis of the Conformations of the HIV-1 Protease from a Large Crystallographic Data Set

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Journal Data Brief
Date 2017 Nov 11
PMID 29124093
Citations 5
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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].

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