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

Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions.

Biochemical and biophysical research communications - 7 Jan 2011

Zhang Yanfeng, Buchko Garry W, Qin Ling, Robinson Howard, Varnum Susan M

Abstract excerpt

The botulinum neurotoxins (BoNTs) produced by different strains of the bacterium Clostridium botulinum are responsible for the disease botulism and include a group of immunologically distinct serotypes (A, B, E, and F) that are considered to be the most lethal natural proteins known for humans. Two BoNT serotypes, C and D, while rarely associated with human infection, are responsible for deadly botulism outbreaks...

Read the complete abstract on PubMed

Topics

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

Share to Botulinum Toxins
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Liposomes

Share to Lysine

Share to Phosphatidylethanolamines

Share to Phospholipids

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 21130733
DOI: 10.1016/j.bbrc.2010.11.134
PMCID: PMC3019264

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions.PMID 21130733Read ↗

A Comprehensive Structural Analysis of Clostridium botulinum Neurotoxin A Cell-Binding Domain from Different SubtypesSemantic proximity Read ↗

Characterization of a membrane binding loop leads to engineering botulinum neurotoxin B with improved therapeutic efficacy.Semantic proximity Read ↗

Two VHH Antibodies Neutralize Botulinum Neurotoxin E1 by Blocking Its Membrane Translocation in Host Cells.Semantic proximity Read ↗

Light Chain Diversity among the Botulinum NeurotoxinsSemantic proximity Read ↗

Structural basis of botulinum neurotoxin serotype A1 binding to human SV2A or SV2C receptorsSemantic proximity Read ↗

Identification of the SV2 protein receptor-binding site of botulinum neurotoxin type E.Semantic proximity Read ↗

The Light Chain Defines the Duration of Action of Botulinum Toxin Serotype A SubtypesSemantic proximity Read ↗

Botulinum Toxin: A Comprehensive Review of Its Molecular Architecture and Mechanistic ActionSemantic proximity Read ↗

Probing the structure and function of the protease domain of botulinum neurotoxins using single-domain antibodiesSemantic proximity Read ↗

Structure of a Bimodular Botulinum Neurotoxin Complex Provides Insights into Its Oral ToxicitySemantic proximity Read ↗

The Molecular Architecture and Mode of Action of Clostridium perfringens ε-ToxinSemantic proximity Read ↗

Structure of Botulinum Neurotoxin Type D Light Chain at 1.65 Å Resolution: Repercussions for VAMP-2 Substrate Specificity<sup>,</sup>Semantic proximity Read ↗

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