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R756G

Category 4 — Stable Fold, Function DisruptedLikely pathogenicLumenal · predictedσ-1 candidateEditorial
ArginineGlycine at position 756 · C-terminal lumenal domain (653-869) · WFS1 (Wolframin)

Arginine → Glycine at position 756 in wolframin's C-terminal lumenal domain. ClinVar Likely pathogenic for Wolfram syndrome 1. AlphaMissense 0.317 (below threshold) — AM under-call. DynaMut2 ΔΔG -0.71 kcal/mol (destabilising). Charge loss + side-chain loss entirely.

Interactive 3D Structure

Wild-type reference
Wild-type R756 — ionic bond to E752
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DynaMut2 mutant · R756G
Mutant G756 — ionic bond to E752 lost (2 contacts lost)
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Bond changes · DynaMut2 interaction analysis

2 lost1 gained7 preserved
Interaction typeWild-type partnerMutant partnerStatus
Ionic bondE752Lost
Hydrogen bondE752E752Preserved
Hydrogen bondE753E753Preserved
Hydrogen bondL759L759Preserved
Polar contactE752E752Preserved
Polar contactE753E753Preserved
Polar contactK758Lost
Polar contactL759L759Preserved
Van der WaalsL754Gained
Van der WaalsK758K758Preserved

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
-0.71kcal/mol
Destabilising — mild
AlphaMissense
0.317
LBen
AlphaFold pLDDT
83
model confidence
Schema
Cat 4
Category 4 — Stable Fold, Function Disrupted

Clinical Evidence

ClinVar classificationLikely pathogenic
Review statuscriteria provided, single submitter
Associated conditionsWolfram syndrome 1
InheritanceWolfram syndrome 1 (AR) documented.
Population frequency (gnomAD v4)Absent from gnomAD v4
cDNA changec.2266C>G
ClinVar accessionVCV003338037
Last evaluated2024/08/20 00:00

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

Structural Context

Position 756 sits in wolframin's C-terminal lumenal domain. The AlphaFold model places R756 within 5 Å of LEU757 (2.5 Å), CYS755 (2.5 Å — potential disulfide site), GLU753 (3.7 Å — likely salt-bridge partner), GLU752 (4.0 Å — second nearby glutamate), and LYS758 (4.4 Å).

The wild-type arginine sits in a charge-rich environment — likely forming a salt bridge with E753 or E752, contributing positive charge to the local electrostatic surface. Replacing R756 with glycine eliminates both the charge and the side chain, leaving a cavity and disrupting the E752/E753 salt-bridge network.

The |ΔΔG| of 0.71 reflects substantial fold cost. AlphaMissense's 0.317 is below threshold — AM under-call. ClinVar Pathogenic + Wolfram 1 confirms clinical pathogenicity.

Amino-acid chemistry
Arginine (R) → Glycine (G) — large positively-charged guanidinium replaced by smallest amino acid. Complete loss of charge and side chain.
Position in the protein
C-terminal lumenal domain · position 756 in the ER lumen (pLDDT 83).

Druggability Assessment

Category 3/4 — Most Druggable (AM under-call). |ΔΔG| = 0.71 — fold survives. AlphaMissense 0.317 below threshold but ClinVar + Wolfram 1 confirm pathogenicity.

Mechanism is loss of R756-E752/E753 salt-bridge network. Therapeutic strategy: site-directed at the E752-E753 microregion.

Why this matters

R756G is another AM-under-call variant with substantial ΔΔG signal. The class continues to grow — variants where structure-based analysis catches what AM training does not.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the R756G 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 R756G PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Topological domain653869 · Lumenal