Literature summary for 3.4.23.47 extracted from

Chen, J.; Liang, Z.; Wang, W.; Yi, C.; Zhang, S.; Zhang, Q.
Revealing origin of decrease in potency of darunavir and amprenavir against HIV-2 relative to HIV-1 protease by molecular dynamics simulations (2014), Sci. Rep., 4, 6872.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations in complerx with inhibitors amprenvir and darunavir	HIV-2 subtype A

Inhibitors

Inhibitors	Comment	Organism	Structure
amprenavir	inhibitor binds less strongly to HIV-2 protease than to HIV-2 protease due to a reduction of the van der Waals interactions. Inhibitor binding tends to make the flaps of PR2 close and the one of PR1 open	HIV-2 subtype A
darunavir	inhibitor binds less strongly to HIV-2 protease than to HIV-2 protease due to a reduction of the van der Waals interactions. Inhibitor binding tends to make the flaps of PR2 close and the one of PR1 open	HIV-2 subtype A

Organism

Organism	UniProt	Comment	Textmining
HIV-2 subtype A	P04584	-	-

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Release 2023.1 (January 2023)