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

Role of the Tryptophan Residues in the Specific Interaction of the Sea Anemone Stichodactyla helianthus's Actinoporin Sticholysin II with Biological Membranes.

Biochemistry - 22 Nov 2016

García-Linares Sara, Maula Terhi, Rivera-de-Torre Esperanza, Gavilanes José G, Slotte J Peter, Martínez-Del-Pozo Álvaro

Abstract excerpt

Actinoporins are pore-forming toxins from sea anemones. Upon interaction with sphingomyelin-containing bilayers, they become integral oligomeric membrane structures that form a pore. Sticholysin II from Stichodactyla helianthus contains five tryptophans located at strategic positions; its role has now been studied using different mutants. Results show that W43 and W115 play a determinant role in maintaining the...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Cytotoxins

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

Share to Hydrogen Bonding

Share to Hydrophobic and Hydrophilic Interactions

Share to Protein Domains

Share to Protein Stability

Share to Sphingomyelins

Share to Tryptophan

Source

Identifiers

PMID: 27933775
DOI: 10.1021/acs.biochem.6b00935

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

Role of the Tryptophan Residues in the Specific Interaction of the Sea Anemone Stichodactyla helianthus's Actinoporin Sticholysin II with Biological Membranes.PMID 27933775Read ↗

Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin's pore assembly.Semantic proximity Read ↗

Validation of a mutant of the pore-forming toxin sticholysin-I for the construction of proteinase-activated immunotoxins.Semantic proximity Read ↗

Cys mutants in functional regions of Sticholysin I clarify the participation of these residues in pore formation.Semantic proximity Read ↗

1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II.Semantic proximity Read ↗

Membrane insertion of the N-terminal alpha-helix of equinatoxin II, a sea anemone cytolytic toxin.Semantic proximity Read ↗

(1)H, (13)C, and (15)N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II.Semantic proximity Read ↗

Structure-function studies of tryptophan mutants of equinatoxin II, a sea anemone pore-forming protein.Semantic proximity Read ↗

Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich.Semantic proximity Read ↗

Fluorescence spectroscopy of soluble E. coli SPase I Δ2-75 reveals conformational changes in response to ligand binding.Semantic proximity Read ↗

Silent mutations at the 5'-end of the cDNA of actinoporins from the sea anemone Stichodactyla helianthus allow their heterologous overproduction in Escherichia coli.Semantic proximity Read ↗

Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes.Semantic proximity Read ↗

Phenotypic selection and characterization of randomly produced non-haemolytic mutants of the toxic sea anemone protein sticholysin II.Semantic proximity Read ↗

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