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Publication Abstract from PubMed

Crystal structures of inactive variants of HIV-1 protease bound to peptides have revealed how the enzyme recognizes its endogenous substrates. The best of the known substrates is, however, a nonnatural substrate that was identified by directed evolution. The crystal structure of the complex between this substrate and the D25N variant of the protease is reported at a resolution of 1.1 A. The structure has several unprecedented features, especially the formation of additional hydrogen bonds between the enzyme and the substrate. This work expands the understanding of molecular recognition by HIV-1 protease and informs the design of new substrates and inhibitors.

A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease.,Windsor IW, Raines RT Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):690-694. doi:, 10.1107/S2059798318006691. Epub 2018 Jun 27. PMID:29968678^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.