Literature summary for 3.4.23.16 extracted from

Liu, F.; Kovalevsky, A.Y.; Louis, J.M.; Boross, P.I.; Wang, Y.F.; Harrison, R.W.; Weber, I.T.
Mechanism of drug resistance revealed by the crystal structure of the unliganded HIV-1 protease with F53L mutation (2006), J. Mol. Biol., 358, 1191-1199.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant mutant F53L, hanging drop vapour diffusion method, X-ray diffraction and analysis at 1.35 A resolution	Human immunodeficiency virus 1

Protein Variants

Protein Variants	Comment	Organism
F53L	site-directed mutagenesis in the flexible flap region, the mutation leads to 15% reduced catalytic efficiency, 20fold higher resistance against indinavir, and reduced dimer stability	Human immunodeficiency virus 1

Inhibitors

Inhibitors	Comment	Organism	Structure
indinavir	drug used in AIDS therapy, mechanism of drug resistance, overview	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	i.e. HIV-1	-

Subunits

Subunits	Comment	Organism
dimer	-	Human immunodeficiency virus 1

Synonyms

Synonyms	Comment	Organism
HIV-1 PR	-	Human immunodeficiency virus 1
HIV-1 protease	-	Human immunodeficiency virus 1

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Release 2023.1 (January 2023)