Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A phenylnorstatine inhibitor binding to HIV-1 protease: geometry, protonation, and subsite-pocket interactions analyzed at atomic resolution.

Journal of medicinal chemistry - 8 Apr 2004

Brynda Jiri, Rezacova Pavlina, Fabry Milan, Horejsi Magdalena, Stouracova Renata, Sedlacek Juraj, Soucek Milan, Hradilek Martin, Lepsik Martin, Konvalinka Jan

Abstract excerpt

The X-ray structure of a complex of HIV-1 protease (PR) with a phenylnorstatine inhibitor Z-Pns-Phe-Glu-Glu-NH(2) has been determined at 1.03 A, the highest resolution so far reported for any HIV PR complex. The inhibitor shows subnanomolar K(i) values for both the wild-type PR and the variant representing one of the most common mutations linked to resistance development. The structure comprising the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Resistance, Viral

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to Phenylbutyrates

Share to Stereoisomerism

Share to Thermodynamics

Source

Identifiers

PMID: 15056001
DOI: 10.1021/jm031105q

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A phenylnorstatine inhibitor binding to HIV-1 protease: geometry, protonation, and subsite-pocket interactions analyzed at atomic resolution.PMID 15056001Read ↗

Electrostatics Plays a Crucial Role in HIV-1 Protease Substrate Binding, Drugs Fail to Take Advantage.Semantic proximity Read ↗

Rational design of inhibitors for drug-resistant HIV-1 aspartic protease mutants.Semantic proximity Read ↗

An allosteric modulator of HIV-1 protease shows equipotent inhibition of wild-type and drug-resistant proteases.Semantic proximity Read ↗

Combination of non-natural D-amino acid derivatives and allophenylnorstatine-dimethylthioproline scaffold in HIV protease inhibitors have high efficacy in mutant HIV.Semantic proximity Read ↗

Pentacycloundecane-based inhibitors of wild-type C-South African HIV-protease.Semantic proximity Read ↗

Structural and kinetic analysis of pyrrolidine-based inhibitors of the drug-resistant Ile84Val mutant of HIV-1 protease.Semantic proximity Read ↗

Structure of a G48H mutant of HIV-1 protease explains how glycine-48 replacements produce mutants resistant to inhibitor drugs.Semantic proximity Read ↗

HIV-1 protease mutations and inhibitor modifications monitored on a series of complexes. Structural basis for the effect of the A71V mutation on the active site.Semantic proximity Read ↗

Structure-activity relationships of novel HIV-1 protease inhibitors containing the 3-amino-2-chlorobenzoyl-allophenylnorstatine structure.Semantic proximity Read ↗

Unique features in the structure of the complex between HIV-1 reverse transcriptase and the bis(heteroaryl)piperazine (BHAP) U-90152 explain resistance mutations for this nonnucleoside inhibitor.Semantic proximity Read ↗

Interactions of different inhibitors with active-site aspartyl residues of HIV-1 protease and possible relevance to pepsin.Semantic proximity Read ↗

Highly conserved glycine 86 and arginine 87 residues contribute differently to the structure and activity of the mature HIV-1 protease.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.