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

Relation between sequence and structure of HIV-1 protease inhibitor complexes: a model system for the analysis of protein flexibility.

Journal of molecular biology - 4 Jan 2002

Zoete V, Michielin O, Karplus M

Abstract excerpt

The flexibility of different regions of HIV-1 protease was examined by using a database consisting of 73 X-ray structures that differ in terms of sequence, ligands or both. The root-mean-square differences of the backbone for the set of structures were shown to have the same variation with residue number as those obtained from molecular dynamics simulations, normal mode analyses and X-ray B-factors. This supports...

Read the complete abstract on PubMed

Topics

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

Share to Consensus Sequence
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Databases, Protein

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to Ligands

Share to Motion

Share to Pliability

Source

Identifiers

PMID: 11771964
DOI: 10.1006/jmbi.2001.5173

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

Relation between sequence and structure of HIV-1 protease inhibitor complexes: a model system for the analysis of protein flexibility.PMID 11771964Read ↗

Effect of structural stress on the flexibility and adaptability of HIV-1 protease.Semantic proximity Read ↗

Relation between flexibility and positively selected HIV-1 protease mutants against inhibitors.Semantic proximity Read ↗

Exploring the conformational landscapes of HIV protease structural ensembles using principal component analysis.Semantic proximity Read ↗

Prediction of mutational tolerance in HIV-1 protease and reverse transcriptase using flexible backbone protein design.Semantic proximity Read ↗

Rigidity, normal modes and flexible motion of a SARS-CoV-2 (COVID-19) protease structureSemantic proximity Read ↗

Structural basis for the resilience of Darunavir (TMC114) resistance major flap mutations of HIV-1 protease.Semantic proximity Read ↗

Studies on flexibility and binding affinity of Asp25 of HIV-1 protease mutants.Semantic proximity Read ↗

Structure-based thermodynamic analysis of HIV-1 protease inhibitors.Semantic proximity Read ↗

Recovery of the wild type atomic flexibility in the HIV-1 protease double mutants.Semantic proximity Read ↗

Domain communication in the dynamical structure of human immunodeficiency virus 1 protease.Semantic proximity Read ↗

Unveiling the Impact of Drug-Sensitive Mutations on HIV-1 Protease Dynamics: A Molecular Dynamics Simulation Study of the T12A, L63Q, and H69N Variants.Semantic proximity Read ↗

Molecular dynamics simulations of 14 HIV protease mutants in complexes with indinavir.Semantic proximity Read ↗

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