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A559D

Category 3/4 — Most DruggableLikely pathogenicCytoplasmic · predictedEditorial
AlanineAspartate at position 559 · Connecting loop · WFS1 (Wolframin)

Alanine → Aspartate at position 559 in a connecting loop — sitting immediately adjacent to position 558, the location of the Atlas's flagship R558C variant (the most common WFS1 mutation in the Ashkenazi Jewish population). ClinVar Likely pathogenic. AlphaMissense 0.979, DynaMut2 ΔΔG -0.73 kcal/mol (destabilising). A position-adjacency variant with direct relevance to R558C.

Interactive 3D Structure

Wild-type reference
Wild-type A559 — hydrogen bond to Y563
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DynaMut2 mutant · A559D
Mutant D559 — hydrogen bond contact to L556 lost
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Bond changes · DynaMut2 interaction analysis

1 lost4 gained17 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondS430Gained
Hydrogen bondE431Gained
Hydrogen bondG555G555Preserved
Hydrogen bondL556L556Preserved
Hydrogen bondG562G562Preserved
Hydrogen bondY563Y563Preserved
Polar contactS430S430Preserved
Polar contactE431E431Preserved
Polar contactV434Gained
Polar contactG555G555Preserved
Polar contactL556L556Preserved
Polar contactL557L557Preserved
Polar contactI561I561Preserved
Polar contactG562G562Preserved
Polar contactY563Y563Preserved
CarbonylG562G562Preserved
Van der WaalsE431E431Preserved
Van der WaalsL556Gained
Van der WaalsG562G562Preserved
HydrophobicE431Lost
HydrophobicV434V434Preserved
HydrophobicY563Y563Preserved

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
-0.73kcal/mol
Destabilising — mild
AlphaMissense
0.979
LPath
AlphaFold pLDDT
87
model confidence
Schema
Cat 3/4
Category 3/4 — Most Druggable

Clinical Evidence

ClinVar classificationLikely pathogenic
Review statuscriteria provided, single submitter
Associated conditions(no specific conditions catalogued for A559D — ClinVar Likely pathogenic by review evidence)
InheritanceInheritance not specified in this ClinVar entry. Given the structural overlap with R558C (which shows both AD and AR presentations), A559D likely contributes to the WFS1 spectrum across both inheritance modes.
Population frequency (gnomAD v4)Absent from gnomAD v4
cDNA changec.1676C>A
ClinVar accessionVCV002734643
Last evaluated2023/06/13 00:00

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

Structural Context

Position 559 sits in a connecting loop. The AlphaFold model places A559 within 5 Å of SER560 (2.5 Å), ARG558 (2.5 Å — the residue mutated in R558C, the Atlas flagship variant), GLU431 (3.2 Å), GLY555 (3.7 Å), LEU556 (3.8 Å), and GLY562 (4.4 Å). The proximity to R558 is the most structurally consequential observation: A559 is the immediate sequence neighbor of the Ashkenazi-population variant, and they share a microenvironment in the loop.

The wild-type alanine at 559 contributes minimal side-chain mass and no functional groups. It serves primarily as a steric and conformational spacer between R558 and the rest of the loop. Critically, the wild-type R558 makes ionic contacts with E431 (3.2 Å from A559, suggesting the loop region wraps around an E431 anchor point) — the same kind of contact disrupted in the R558C variant.

Replacing alanine with aspartate at 559 introduces a negatively-charged carboxylate into the loop one residue away from R558. In the wild-type, R558 is positively charged and E431 is negatively charged, and they form a salt bridge. Adding a second negative charge at position 559, immediately adjacent to R558, perturbs this salt-bridge geometry — the new D559 carboxylate competes with E431 for the R558 guanidinium's electrostatic interaction.

DynaMut2 returns |ΔΔG| of 0.73 kcal/mol — the fold survives, but the loop electrostatic network is materially perturbed. AlphaMissense's 0.979 score reflects the high pathogenic potential of disrupting the same salt bridge geometry that R558C also disrupts (from the R558 side rather than the partner side).

Amino-acid chemistry
Alanine (A) → Aspartate (D) — a small hydrophobic methyl-bearing residue replaced by a small negatively-charged carboxylate-bearing residue. The substitution introduces both volume and charge where the wild-type alanine provided neither.
Position in the protein
Connecting loop · position 559 sits one residue downstream of position 558, where the Atlas's most prominent variant R558C is located. Same loop region between TM helices, solvent-accessible.

Druggability Assessment

Category 3/4 — Most Druggable. |ΔΔG| = 0.73 kcal/mol — fold survives. AlphaMissense 0.979 confirms severe functional consequence.

The mechanism is disruption of the R558-E431 salt bridge through an adjacent introduced charge — the same therapeutic surface targeted by R558C. A drug designed to rescue the R558C variant by re-stabilizing the loop's electrostatic network would, in principle, also rescue A559D.

This is the Atlas's clearest demonstration of a 'sister-variant' relationship: two distinct pathogenic substitutions perturbing the same structural feature from different angles. Drug discovery at the R558-E431-A559 microregion has two converging targets.

Why this matters

A559D's proximity to R558C — the most common WFS1 variant in the Ashkenazi Jewish population — makes it strategically important beyond its individual clinical impact. A pharmacological chaperone or small-molecule binder designed for R558C's loop microregion has direct relevance to A559D patients as well. The atlas surfaces this position-adjacency relationship through the neighbor analysis (ARG558 at 2.5 Å from A559); pre-atlas drug discovery would have treated these as unrelated targets.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the A559D 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 A559D PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Natural variant559559 · in dbSNP:rs55814513