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

The Effect of Acidic Residues on the Binding between Opicalcin1 and Ryanodine Receptor from the Structure-Functional Analysis.

Journal of natural products - 26 Jan 2024

Yao Jinchi, Hua Xiaoyu, Huo Wenjing, Xiao Li, Wang Yongfang, Tang Qinglong, Valdivia Carmen R, Valdivia Héctor H, Dong Weibing, Xiao Liang

Abstract excerpt

Calcin is a group ligand with high affinity and specificity for the ryanodine receptors (RyRs). Little is known about the effect of its acidic residues on the spacial structure as well as the interaction with RyRs. We screened the opicalcin1 acidic mutants and investigated the effect of mutation on activity. The results indicated that all acidic mutants maintained the structural features, but their surface charge...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Calcium Signaling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Docking Simulation

Share to Mutation

Share to Ryanodine Receptor Calcium Release Channel

Source

Open in PubMed Open full text

Identifiers

PMID: 38128916
DOI: 10.1021/acs.jnatprod.3c00821
PMCID: PMC10825818

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

The Effect of Acidic Residues on the Binding between Opicalcin1 and Ryanodine Receptor from the Structure-Functional Analysis.PMID 38128916Read ↗

Ryanodine receptors: structure and function.Semantic proximity Read ↗

Evolution of Vertebrate Ryanodine Receptors Family in Relation to Functional Divergence and Conservation.Semantic proximity Read ↗

Recent advances in calcium-sensing receptor structures and signaling pathways.Semantic proximity Read ↗

The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule.Semantic proximity Read ↗

Understanding the molecular functions of the second extracellular loop (ECL2) of the calcitonin gene-related peptide (CGRP) receptor using a comprehensive mutagenesis approach.Semantic proximity Read ↗

A conserved and druggable pocket in class B G protein coupled receptors for orally active small molecule agonistsSemantic proximity Read ↗

High activity of the calcineurin A subunit with a V314 deletion.Semantic proximity Read ↗

Mapping Ryanodine Binding Sites in the Pore Cavity of Ryanodine Receptors.Semantic proximity Read ↗

In-silico screening of missense nsSNPs in Delta-opioid receptor protein and their restoring tendency on MCRT interaction; focusing on dynamic nature.Semantic proximity Read ↗

Opioid Addiction and Opioid Receptor Dimerization: Structural Modeling of the OPRD1 and OPRM1 Heterodimer and Its Signaling Pathways.Semantic proximity Read ↗

Disease mutations in the ryanodine receptor N-terminal region couple to a mobile intersubunit interface.Semantic proximity Read ↗

Two rings of negative charges in the cytosolic vestibule of type-1 ryanodine receptor modulate ion fluxes.Semantic proximity Read ↗

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