A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease.

doi:10.1107/S2059798318006691

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Article

A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease.

Acta crystallographica. Section D, Structural biology - 1 Jul 2018

Windsor Ian W, Raines Ronald T

Abstract excerpt

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...

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Identifiers

PMID: 29968678
DOI: 10.1107/S2059798318006691
PMCID: PMC6038388

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.