ArticleActa crystallographica. Section D, Structural biology2018
A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- ApaH decaps NpNature chemical biology · 2026Article
- Circular zymogens of human ribonuclease 1.Protein science : a publication of the Protein Society · 2019Article
- AnACS catalysis · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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 Å. 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.
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