Structural Shifts of the Parvovirus B19 Capsid Receptor-binding Domain: A Peptide Study.

doi:10.2174/0109298665272845231121064717

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

Community

Back to search

Article

Structural Shifts of the Parvovirus B19 Capsid Receptor-binding Domain: A Peptide Study.

Protein and peptide letters - 1 Jan 2024

Khrustalev Vladislav Victorovich, Stojarov Aleksander Nicolaevich, Akunevich Anastasia Aleksandrovna, Baranov Oleg Evgenyevich, Popinako Anna Vladimirovna, Samoilovich Elena Olegovna, Yermalovich Marina Anatolyevna, Semeiko Galina Valeryevna, Sapon Egor Gennadyevich, Cheprasova Victoria Igorevna, Shalygo Nikolai Vladimirovich, Poboinev Victor Vitoldovich, Khrustaleva Tatyana Aleksandrovna, Khrustaleva Olga Victorovna

Abstract excerpt

BACKGROUND: Binding appropriate cellular receptors is a crucial step of a lifecycle for any virus. Structure of receptor-binding domain for a viral surface protein has to be determined before the start of future drug design projects. OBJECTIVES: Investigation of pH-induced changes in the secondary structure for a capsid peptide with loss of function mutation can shed some light on the mechanism of entrance....

Read the complete abstract on PubMed

Topics

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

Share to Capsid Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Circular Dichroism

Share to Hydrogen-Ion Concentration

Share to Parvovirus B19, Human

Share to Peptides

Share to Protein Domains

Share to Protein Structure, Secondary

Share to Receptors, Virus

Source

Open in PubMed

Identifiers

PMID: 38053353
DOI: 10.2174/0109298665272845231121064717

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

Structural Shifts of the Parvovirus B19 Capsid Receptor-binding Domain: A Peptide Study.PMID 38053353Read ↗

The Receptor-Binding Domain in the VP1u Region of Parvovirus B19.Semantic proximity Read ↗

Conformational Changes in the VP1-Unique Region of Native Human Parvovirus B19 Lead to Exposure of Internal Sequences That Play a Role in Virus Neutralization and InfectivitySemantic proximity Read ↗

The N-Terminal 5-68 Amino Acids Domain of the Minor Capsid Protein VP1 of Human Parvovirus B19 Enters Human Erythroid Progenitors and Inhibits B19 InfectionSemantic proximity Read ↗

The structure of human parvovirus B19Semantic proximity Read ↗

A slender tract of glycine residues is required for translocation of the VP2 protein N-terminal domain through the parvovirus MVM capsid channel to initiate infection.Semantic proximity Read ↗

A Novel Murine Model of Parvovirus Associated Dilated Cardiomyopathy Induced by Immunization with VP1-Unique Region of Parvovirus B19.Semantic proximity Read ↗

His-Trp cation-π interaction and its structural role in an α-helical dimer of HIV-1 Vpr protein.Semantic proximity Read ↗

The VP1-unique region of parvovirus B19: amino acid variability and antigenic stability.Semantic proximity Read ↗

Structural tolerance versus functional intolerance to mutation of hydrophobic core residues surrounding cavities in a parvovirus capsid.Semantic proximity Read ↗

Structure of the Diphtheria Toxin at Acidic pH: Implications for the Conformational Switching of the Translocation Domain.Semantic proximity Read ↗

Temperature inducible beta-sheet structure in the transactivation domains of retroviral regulatory proteins of the Rev family.Semantic proximity Read ↗

Structural analysis of three peptides related to the transmambranic helix VI of AT1 receptor.Semantic proximity Read ↗

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