Literature summary for 3.4.23.16 extracted from

Tyndall, J.D.; Pattenden, L.K.; Reid, R.C.; Hu, S.H.; Alewood, D.; Alewood, P.F.; Walsh, T.; Fairlie, D.P.; Martin, J.L.
Crystal structures of highly constrained substrate and hydrolysis products bound to HIV-1 protease. Implications for the catalytic mechanism (2008), Biochemistry, 47, 3736-3744.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion, a hexapeptide substrate (containing two macrocyclic tripeptides constrained to mimic alpha/beta-strand conformation, linked by a scissile peptide bond, to probe the structural mechanism of proteolysis) is cocrystallized with catalytically active synthetic HIV-1 protease and an inactive isosteric D25N mutant, and three-dimensional structures are determined by 1.6 A	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

Synonyms

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

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Release 2023.1 (January 2023)