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

Nine crystal structures determine the substrate envelope of the MDR HIV-1 protease.

The protein journal - 1 Mar 2011

Liu Zhigang, Wang Yong, Brunzelle Joseph, Kovari Iulia A, Kovari Ladislau C

Abstract excerpt

Under drug selection pressure, emerging mutations render HIV-1 protease drug resistant, leading to the therapy failure in anti-HIV treatment. It is known that nine substrate cleavage site peptides bind to wild type (WT) HIV-1 protease in a conserved pattern. However, how the multidrug-resistant (MDR) HIV-1 protease binds to the substrate cleavage site peptides is yet to be determined. MDR769 HIV-1 protease...

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
Share to Drug Resistance, Multiple, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Protease

Share to Molecular Conformation

Share to Protein Binding

Share to Substrate Specificity

Source

Identifiers

PMID: 21394574
DOI: 10.1007/s10930-011-9316-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nine crystal structures determine the substrate envelope of the MDR HIV-1 protease.PMID 21394574Read ↗

Conserved hydrogen bonds and water molecules in MDR HIV-1 protease substrate complexes.Semantic proximity Read ↗

Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 angstroms resolution crystal structures of HIV-1 protease mutants with substrate analogs.Semantic proximity Read ↗

HIV-1 protease substrate-groove: Role in substrate recognition and inhibitor resistance.Semantic proximity Read ↗

Contribution of the 80s loop of HIV-1 protease to the multidrug-resistance mechanism: crystallographic study of MDR769 HIV-1 protease variants.Semantic proximity Read ↗

How Mutations Can Resist Drug Binding yet Keep HIV-1 Protease Functional.Semantic proximity Read ↗

"Wide-open" 1.3 A structure of a multidrug-resistant HIV-1 protease as a drug target.Semantic proximity Read ↗

Identification of Structural Mechanisms of HIV-1 Protease Specificity Using Computational Peptide Docking: Implications for Drug ResistanceSemantic proximity Read ↗

Structural, kinetic, and thermodynamic studies of specificity designed HIV-1 protease.Semantic proximity Read ↗

Evaluating the potency of HIV-1 protease drugs to combat resistance.Semantic proximity Read ↗

Studies on adaptability of binding residues and flap region of TMC-114 resistance HIV-1 protease mutants.Semantic proximity Read ↗

Insights into the interaction mechanism of first-generation HIV-1 protease inhibitors with wild-type and mutant (D30N and L76V) enzymes through in-silico based approach.Semantic proximity Read ↗

Highly drug-resistant HIV-1 protease reveals decreased intra-subunit interactions due to clusters of mutations.Semantic proximity Read ↗

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