RareResearch.AI
← Back to atlas

A326E

Category 3/4 — Most DruggableLikely pathogenicTransmembrane · predictedEditorial
AlanineGlutamate at position 326 · TM1 (314-334), helical transmembrane · WFS1 (Wolframin)

Alanine → Glutamate at position 326 inside TM1. ClinVar Likely pathogenic, DFNA6 hearing loss. AlphaMissense 0.940, DynaMut2 ΔΔG -0.33 kcal/mol (destabilising). Charge-introduction variant in TM1.

Interactive 3D Structure

Wild-type reference
Wild-type A326 — hydrogen bond to H322
Fullscreen ↗
DynaMut2 mutant · A326E
Mutant E326 — hydrogen bond contact to H323 lost
Fullscreen ↗

Bond changes · DynaMut2 interaction analysis

1 lost0 gained10 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondH322H322Preserved
Hydrogen bondH323Lost
Hydrogen bondF329F329Preserved
Hydrogen bondF330F330Preserved
Polar contactH322H322Preserved
Polar contactH323H323Preserved
Polar contactI324I324Preserved
Polar contactF329F329Preserved
Polar contactF330F330Preserved
Van der WaalsI324I324Preserved
HydrophobicF330F330Preserved

Lost / gained / preserved interatomic contacts at the variant residue, from the DynaMut2 (Arpeggio) interaction analysis of the wild-type and energy-minimized mutant structures.

Computational Predictions

DynaMut2 ΔΔG
-0.33kcal/mol
Destabilising — mild
AlphaMissense
0.940
LPath
AlphaFold pLDDT
77
model confidence
Schema
Cat 3/4
Category 3/4 — Most Druggable

Clinical Evidence

ClinVar classificationLikely pathogenic
Review statuscriteria provided, single submitter
Associated conditionsAutosomal dominant nonsyndromic hearing loss 6 (DFNA6)
InheritanceDFNA6 hearing loss documented.
Population frequency (gnomAD v4)Absent from gnomAD v4
cDNA changec.977C>A
ClinVar accessionVCV004687962
Last evaluated2025/08/25 00:00

Not observed in ~730k individuals — consistent with a rare allele (ACMG PM2_supporting).

Structural Context

Position 326 sits in TM1. The AlphaFold model places A326 within 5 Å of ASN325 (2.5 Å), LEU327 (2.5 Å), HIS322 (3.6 Å), HIS323 (3.7 Å — partner of H323R Atlas card), and PHE329 (4.2 Å). The local environment includes two adjacent histidines (H322, H323).

Replacing alanine with glutamate introduces a negative charge into the bilayer-embedded TM1 environment. The carboxylate can interact with the nearby H322/H323 imidazoles when they're protonated, potentially forming a stable salt-bridge that differs from the wild-type fold geometry. But this rearrangement comes at a structural cost.

The |ΔΔG| of 0.33 reflects fold accommodation. AlphaMissense's 0.940 + DFNA6 confirm severe functional consequence. Mechanism is charge introduction at the TM1 H322-H323 cluster.

Amino-acid chemistry
Alanine (A) → Glutamate (E) — small methyl-bearing hydrophobic replaced by negatively-charged carboxylate-bearing residue.
Position in the protein
TM1 (residues 314–334) · position 326 mid-helix, bilayer-embedded (pLDDT 77).

Druggability Assessment

Category 3/4 — Most Druggable. |ΔΔG| = 0.33 — fold survives. AlphaMissense 0.940 + DFNA6 confirm severe functional consequence.

Mechanism is charge introduction into the TM1 H322-H323 cluster. Therapeutic strategy: site-directed at TM1 mid-helix.

Why this matters

A326E joins the TM1 variant cluster (W314R, H313Y, H323R, T321R, T321P, A326E). Six variants in or near TM1 in the Atlas — the helix is a recurring therapeutic target region.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the A326E PDF below and upload it to Wolfram Intelligence to generate therapeutic-strategy proposals — guanidinium mimetics, sigma-1 agonist docking, NAC thiol-capping. NAC is already on the bench-testing list.

Download A326E PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Transmembrane314334 · Helical
Natural variant326326 · in dbSNP:rs369795224