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

Thermal stability of the K+ channel tetramer: cation interactions and the conserved threonine residue at the innermost site (S4) of the KcsA selectivity filter.

Biochemistry - 13 May 2008

Krishnan Manoj N, Trombley Patrick, Moczydlowski Edward G

Abstract excerpt

The selectivity filter of most K+ channels contains a highly conserved Thr residue that uniquely forms the S4 binding site for K+ by dual coordination with the backbone carbonyl oxygen and side chain hydroxyl of the same residue. This study examines the effect of mutations of Thr75 in the S4 site of theKcsA K+ channel on the cation dependence of the thermal stability of the tetramer, a phenomenon that reflects...

Read the complete abstract on PubMed

Topics

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

Share to Cations
Share to Conserved Sequence

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

Share to Dimerization

Share to Potassium Channels

Share to Protein Denaturation

Share to Sensitivity and Specificity

Share to Sulfhydryl Compounds

Share to Threonine

Source

Identifiers

PMID: 18419132
DOI: 10.1021/bi702281p

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

Thermal stability of the K+ channel tetramer: cation interactions and the conserved threonine residue at the innermost site (S4) of the KcsA selectivity filter.PMID 18419132Read ↗

Ion binding to KcsA: implications in ion selectivity and channel gating.Semantic proximity Read ↗

A mutant KcsA K(+) channel with altered conduction properties and selectivity filter ion distribution.Semantic proximity Read ↗

Potassium-selective block of barium permeation through single KcsA channels.Semantic proximity Read ↗

Ionic interactions of Ba2+ blockades in the MthK K+ channel.Semantic proximity Read ↗

Individual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation.Semantic proximity Read ↗

Structural and functional consequences of an amide-to-ester substitution in the selectivity filter of a potassium channel.Semantic proximity Read ↗

K⁺ channel gating: C-type inactivation is enhanced by calcium or lanthanum outside.Semantic proximity Read ↗

P-loop flexibility in Na+ channel pores revealed by single- and double-cysteine replacements.Semantic proximity Read ↗

Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.Semantic proximity Read ↗

Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites.Semantic proximity Read ↗

Outer pore architecture of a Ca2+-selective TRP channel.Semantic proximity Read ↗

Mutations in the K(+)-channel KcsA toward Kir channels alter salt-induced clusterization and blockade by quaternary alkylammonium ions.Semantic proximity Read ↗

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