Literature summary for 3.4.23.16 extracted from

Kozisek, M.; Saskova, K.G.; Rezacova, P.; Brynda, J.; van Maarseveen, N.M.; De Jong, D.; Boucher, C.A.; Kagan, R.M.; Nijhuis, M.; Konvalinka, J.
Ninety-nine is not enough: molecular characterization of inhibitor resistant HIV-1 protease mutants with insertions in the flap region (2008), J. Virol., 82, 5869-5878.

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Application

Application	Comment	Organism
medicine	insertions at positions 33 and 35 contribute to the viral resistance to most of the tested protease inhibitors. The structural analysis reveals local structural rearrangements in the flap region and in the substrate binding pockets. The enlargement of the HIV proteinase substrate binding site together with impaired flap dynamics could account for the weaker inhibitor binding by the insertion mutants. Amino acid insertions in the vicinity of the binding cleft represent a mechanism of HIV resistance development	Human immunodeficiency virus 1

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of variants of HIV proteinase with or without insertions at positions 33 and 35	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	P03367	-	-

Synonyms

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

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Release 2023.1 (January 2023)