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

Molecular dynamics and ligand docking of a hinge region variant of South African HIV-1 subtype C protease.

Journal of molecular graphics & modelling - 1 Jun 2018

Zondagh Jake, Balakrishnan Vijayakumar, Achilonu Ikechukwu, Dirr Heini W, Sayed Yasien

Abstract excerpt

HIV-1 protease is an important antiretroviral drug target due to its key role in viral maturation. Computational models have been successfully used in the past to understand the dynamics of HIV-1 protease variants. We performed molecular dynamics simulations and induced fit docking on a wild-type South African HIV-1 subtype C protease and an N37T↑V hinge region variant. The simulations were initiated in a cubic...

Read the complete abstract on PubMed

Topics

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

Share to South Africa
Share to HIV Protease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Protease Inhibitors

Share to Molecular Conformation

Share to Molecular Docking Simulation

Share to Molecular Dynamics Simulation

Share to Protein Interaction Domains and Motifs

Share to Quantitative Structure-Activity Relationship

Source

Identifiers

PMID: 29625416
DOI: 10.1016/j.jmgm.2018.03.006

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

Molecular dynamics and ligand docking of a hinge region variant of South African HIV-1 subtype C protease.PMID 29625416Read ↗

Cantilever-centric mechanism of cooperative non-active site mutations in HIV protease: Implications for flap dynamics.Semantic proximity Read ↗

Exploring the flap dynamics of the South African HIV subtype C protease in presence of FDA-approved inhibitors: MD study.Semantic proximity Read ↗

Structural insights into the South African HIV-1 subtype C protease: impact of hinge region dynamics and flap flexibility in drug resistanceSemantic proximity Read ↗

Contrasting the effect of hinge region insertions and non-active site mutations on HIV protease-inhibitor interactions: Insights from altered flap dynamics.Semantic proximity Read ↗

The impact of active site mutations of South African HIV PR on drug resistance: Insight from molecular dynamics simulations, binding free energy and per-residue footprints.Semantic proximity Read ↗

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

Drug Resistance Mutations Alter Dynamics of Inhibitor-Bound HIV-1 ProteaseSemantic proximity Read ↗

Multiple Molecular Dynamics Simulations and Free-Energy Predictions Uncover the Susceptibility of Variants of HIV-1 Protease against Inhibitors Darunavir and KNI-1657.Semantic proximity Read ↗

Differential Flap Dynamics in Wild-Type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR RelaxationSemantic proximity Read ↗

Molecular dynamics studies on HIV-1 protease: a comparison of the flap motions between wild type protease and the M46I/G51D double mutant.Semantic proximity Read ↗

HIV Protease Hinge Region Insertions at Codon 38 Affect Enzyme Kinetics, Conformational Stability and Dynamics.Semantic proximity Read ↗

Restrained molecular dynamics simulations of HIV-1 protease: the first step in validating a new target for drug design.Semantic proximity Read ↗

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