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R558H

Category 3/4 — Most DruggablePathogenic/Likely pathogenicCytoplasmic · predictedEditorial
ArginineHistidine at position 558 · Connecting loop · WFS1 (Wolframin)

Same residue as the Atlas's R558C pilot variant, different substitution — arginine retained as histidine, a partial charge swap that preserves the side chain's polar character but loses ~80% of the wild-type positive charge at physiological pH.

Expert Review · corrections applied

Reviewed by an affected-family domain expert

The card's structural prose concluded that because R558H lacks R558C's free-thiol oxidative-stress liability, 'clinically, the consequence is that R558H may present with somewhat milder disease.' That is a phenotype claim generalized from a neighbouring variant at the same residue, which the Gladstone review prohibits: structural similarity supports a mechanistic hypothesis, never a phenotype claim. There is no published R558H cohort data on the card to support a severity statement. The mechanistic comparison is retained; the clinical inference is removed and replaced with an explicit statement that presentation does not follow from the structural comparison. Found by an Atlas-wide prose scan while shipping v2 — this was the only instance of cross-variant phenotype generalization in the 2,085-variant corpus.

Dr. Sarah Gladstone · 2026-08-14 · Gladstone v2 policy entry 4 (phenotype generalization)

Full corrections log →

Interactive 3D Structure

Wild-type reference
Wild-type R558 — ionic bond to E431
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DynaMut2 mutant · R558H
Mutant H558 — ionic bond to E431 lost (3 contacts lost)
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Bond changes · DynaMut2 interaction analysis

3 lost1 gained6 preserved
Interaction typeWild-type partnerMutant partnerStatus
Ionic bondE431Lost
Hydrogen bondE431Lost
Hydrogen bondL554L554Preserved
Hydrogen bondG555G555Preserved
Hydrogen bondG562G562Preserved
Polar contactE431Lost
Polar contactL554L554Preserved
Polar contactG555G555Preserved
Polar contactG562G562Preserved
Van der WaalsL556Gained

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
-1.31kcal/mol
Destabilising — moderate
AlphaMissense
0.760
LPath
AlphaFold pLDDT
85
model confidence
Schema
Cat 3/4
Category 3/4 — Most Druggable
ΔΔG confidence: Standard confidence · Cytoplasmic

This variant is in a water-facing region, which is the regime the stability predictor was built and benchmarked for. Ordinary predictor error still applies.

Clinical Evidence

ClinVar classificationPathogenic/Likely pathogenic
Review statuscriteria provided, multiple submitters, no conflicts
Associated conditionsWolfram syndrome 1; Wolfram-like syndrome; WFS1-related disorder; Autosomal dominant nonsyndromic hearing loss 6; Optic atrophy; Cataract 41; Type 2 diabetes mellitus; Inborn genetic diseases
InheritanceBoth autosomal dominant and autosomal recessive forms documented.
Population frequency (gnomAD v4)Ultra-rare · AF 0.0077%
cDNA changec.1673G>A
ClinVar accessionVCV000427051
Last evaluated2025/11/23 00:00

Observed at very low frequency in gnomAD.

Classified for2★ documented assertion

ClinVar classifies this variant as Pathogenic/Likely pathogenic for Optic atrophy / optic neuropathy (autosomal dominant); Wolfram syndrome (classic) (autosomal recessive, OMIM 222300); Cataract 41 (autosomal dominant, OMIM 116400); Nonsyndromic hearing loss (DFNA6/14/38) (autosomal dominant, OMIM 600965); WFS1-related diabetes (autosomal dominant); Wolfram-like syndrome (autosomal dominant, OMIM 614296); WFS1-related spectrum (unresolved mode) (dominant or recessive). ClinVar records this under a WFS1-spectrum label that spans both disease families — recessive Wolfram syndrome (biallelic) and the dominant WFS1-related disorders. The label does not resolve which applies, and it is not a severity statement.

  • Optic atrophy / optic neuropathyautosomal dominantsubmitted as: Optic atrophy
  • Wolfram syndrome (classic)autosomal recessive · OMIM 222300submitted as: Wolfram syndrome 1; Wolfram syndrome 1; Wolfram syndrome; Wolfram syndrome 1
  • Cataract 41autosomal dominant · OMIM 116400submitted as: Cataract 41
  • Nonsyndromic hearing loss (DFNA6/14/38)autosomal dominant · OMIM 600965submitted as: Autosomal dominant nonsyndromic hearing loss 6; Autosomal dominant nonsyndromic hearing loss 6
  • WFS1-related diabetesautosomal dominantsubmitted as: Type 2 diabetes mellitus
  • Wolfram-like syndromeautosomal dominant · OMIM 614296submitted as: Wolfram-like syndrome
  • WFS1-related spectrum (unresolved mode)dominant or recessivesubmitted as: WFS1-related disorder
  • Phenotype scope is interpretation of submitted records. The computed values on this card (AlphaMissense, DynaMut2 ΔΔG, pLDDT) are measurements of the model, not of a patient.
  • Presentation cannot be generalised from neighbouring variants: one nucleotide over can present very differently. Structural similarity supports a mechanistic hypothesis, never a phenotype claim.

Review status: 2★ multiple submitters, no conflicts. ClinVar "conditions" is the union of all submissions; 0–1★ entries are submitted conditions, not documented phenotypes.

Population frequency
Global (all ancestries)
AF 0.0077% · 124 / 1,612,718 alleles
Homozygotes
0
Highest-frequency population
European (non-Finnish) · AF 0.0092%

Highest in European (non-Finnish): AF 0.0092% (108 of 1,180,042 alleles), in line with the global figure.

No homozygotes reported in gnomAD v4. For a recessive allele this is expected and is not, on its own, evidence either way.

Ancestry groupAllele freq.AC / ANHom.Carrier est.
European (non-Finnish)0.0092%108 / 1,180,0420~1 in 5460
Admixed American0.0083%5 / 60,0140~1 in 6000
East Asian0.0067%3 / 44,8940~1 in 7480
South Asian0.0044%4 / 91,0840~1 in 11390
African / African American0.0040%3 / 74,9460~1 in 12490
Remaining individuals · under-sampled0.0016%1 / 62,4700

Source: gnomAD r4, retrieved 2026-08-21. Values are allele frequencies. The carrier estimate is derived from the allele frequency (Hardy-Weinberg, ~2·AF) and is an approximation, not a published figure — where a published carrier frequency exists it outranks this column and is cited on the card.

Structural Context

R558 sits at the cytoplasmic edge of the membrane interface, 5 residues before the start of TM8. The structural neighbors here are: Ala559 (2.45 Angstrom), Leu557 (2.47 Angstrom), Gly555 (3.63 Angstrom), Leu554 (3.82 Angstrom), Leu556 (4.50 Angstrom), Ser560 (4.61 Angstrom), Ile561 (4.81 Angstrom), and Gly562 (4.90 Angstrom). The cluster is dominated by hydrophobic residues — three leucines, one alanine, one isoleucine, two glycines — and a single polar serine. The wild-type arginine's guanidinium therefore projects outward into solvent or toward an anionic phospholipid headgroup, while its long aliphatic stem packs against the surrounding leucine/alanine cluster.

Replacing arginine with histidine removes the full positive charge but retains a polar imidazole. At cytoplasmic pH (~7.2), histidine is predominantly neutral (~10% protonated). The electrostatic anchor to anionic lipid headgroups is lost. The long aliphatic stem of arginine, which contributes hydrophobic packing against the surrounding leucines, is also lost — histidine's side chain is much shorter (~4 Angstrom vs ~6 Angstrom). The combined effect is geometric: histidine cannot reach the same packing partners as arginine, and the local cluster loses both an electrostatic and a hydrophobic contribution.

DynaMut2's DeltaDeltaG of -1.31 kcal/mol is a clean read of this combined loss — somewhat larger than R558C's -0.5 kcal/mol, consistent with histidine being a more conservative substitution chemically but geometrically more disruptive because of the side-chain length mismatch. AlphaMissense scores R558H at 0.760 (LPath) — pathogenic but notably lower than R558C's 0.849, reflecting the imidazole's partial retention of polar character.

Cross-reference to the R558C pilot card: both variants disrupt the same anchor at the TM7-TM8 cytoplasmic loop. R558C loses the positive charge and adds a free thiol with potential disulfide-formation risk. R558H loses ~90% of the positive charge but adds no covalent-modification liability. The two variants therefore share most of their molecular phenotype but diverge in one respect — R558C carries an additional oxidative-stress vulnerability that R558H does not. That is a mechanistic difference, and it stops there: no clinical inference about R558H's presentation or severity follows from it. Presentation cannot be generalised from a neighbouring variant, even at the same residue — one substitution over can present very differently, and there is no published R558H cohort data on this card to support a severity claim. Both are classified Pathogenic/Likely pathogenic; what that means for a given person is not settled by the structural comparison above. (Corrected 2026-08-21 on expert review — Dr. Sarah Gladstone, 2026-08-14: phenotype generalization across variants.)

Amino-acid chemistry
Arginine (large, positively charged, fully ionized guanidinium at physiological pH, pKa ~12.5) to Histidine (smaller, imidazole side chain with pKa ~6.0 — mostly neutral at physiological pH, partially positive in acidic compartments) at position 558.
Position in the protein
Position 558 sits in a cytoplasmic connecting loop between TM7 (residues 529-549) and TM8 (residues 563-583) — the same residue position as the Atlas's R558C pilot variant. pLDDT 84.56 (identical to R558C since they share the wild-type AlphaFold structure) confirms the position is well-modeled and not in an IDR.

Druggability Assessment

Final classification: Category 3 — Most Druggable. The convergent evidence: pLDDT 84.56 (ordered, modelable), DeltaDeltaG magnitude 1.31 kcal/mol (mild-moderate, fold-intact), AlphaMissense 0.760 (pathogenic), and direct structural parallel to the R558C pilot. The therapeutic target is the same cytoplasmic anchor between TM7 and TM8. A pharmacological chaperone designed against R558C should be directly tested against R558H — the two variants share the same loss-of-anchor mechanism, and any small molecule that restores the wild-type cytoplasmic loop geometry should rescue both. R558H is therefore a high-priority companion variant in any R558C-directed screening program. The shared chemistry argument is the kind of cross-variant leverage the Atlas exists to surface.

Why this matters

R558H is the second variant in the Atlas at position 558 — the same locus that produces the Ashkenazi-Jewish founder mutation R558C. Both variants disrupt the same TM7-TM8 cytoplasmic anchor. This is exactly the cross-residue-substitution insight the Atlas was built to expose: position 558 is mechanistically a single therapeutic target, and a chaperone screen designed against the wild-type R558 geometry should produce hits useful for both R558C and R558H carriers. The broader Atlas strategy implication is that variant clusters at the same residue position deserve unified druggability assessment. Position 558 is the first clear example. Similar logic should apply to other multi-substitution residues (e.g., G674 with at least four substitutions in the Atlas) — these are not three separate problems, they are one site with three failure modes.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the R558H 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 R558H PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Natural variant558558 · in WFS1; dbSNP:rs199946797