Article

An allosteric pocket in K <sub>V</sub> 1.3 defines a distinct chemical space for immunomodulator design

2026-07-07

Abstract excerpt

K V 1.3 is a validated autoimmune drug target, yet all disclosed inhibitors converge on a narrow set of conserved binding sites, suffering from poor selectivity or clinical failure. Whether K V 1.3 harbors a distinctive, druggable pocket amenable to selective targeting has remained unknown. Here we report MPiN, a highly selective, state-dependent K V 1.3 inhibitor with in vivo efficacy in a mouse psoriasis mode...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 92f7b29e-c666-5680-81de-b9e00def168a
DOI: 10.64898/2026.07.06.736759

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

An allosteric pocket in K <sub>V</sub> 1.3 defines a distinct chemical space for immunomodulator designDOI 10.64898/2026.07.06.736759Read

An allosteric pocket in KV1.3 defines a distinct chemical space for immunomodulator designSemantic proximity Read

Stereoselectivity and functional plasticity of a common ligand-binding pocket in TRPM3Semantic proximity Read

Kv1.3 in the spotlight for treating immune diseasesSemantic proximity Read

Stereoselectivity and functional plasticity of a common ligand-binding pocket in TRPM3.Semantic proximity Read

A generic binding pocket for small molecule <i> I <sub>Ks</sub> </i> activators at the extracellular inter-subunit interface of KCNQ1 and KCNE1 channel complexesSemantic proximity Read

Mutation-Induced Pocket Deactivation: How Ser353/Pro245 Alters K <sub>Ca</sub> 2.2 vs K <sub>Ca</sub> 3.1 Ligand SelectivitySemantic proximity Read

Mutation-Induced Pocket Deactivation: How Ser353/Pro245 Alters KCa2.2 vs. KCa3.1 Ligand Selectivity.Semantic proximity Read

A unique lower X-gate in TASK channels traps inhibitors within the vestibuleSemantic proximity Read

Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gatingSemantic proximity Read

Discovery of Kv3.1 channel inhibitors reveals VU0521426 as a state-dependent inactivator preferentially active against pathogenic gain-of-function mutants.Semantic proximity Read

Structural basis for proton inhibition of the two-pore domain K+ channel TASK-1.Semantic proximity Read

Structural basis for proton inhibition of the two-pore domain K <sup>+</sup> channel TASK-1Semantic proximity Read