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C529R

Category 4 — Stable Fold, Function DisruptedUncertain significanceTransmembrane · predictedSource card
CysteineArginine at position 529 · Cytoplasmic loop 4 · WFS1 (Wolframin)

Interactive 3D Structure

Wild-type reference
Wild-type C529 — hydrogen bond to K525
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DynaMut2 mutant · C529R
Mutant R529 — energy-minimized; 1 new contact formed
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Bond changes · DynaMut2 interaction analysis

0 lost1 gained3 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondK525K525Preserved
Hydrogen bondP533P533Preserved
Polar contactK525K525Preserved
Polar contactP533Gained

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
-0.25kcal/mol
Destabilising — mild
AlphaMissense
0.519
ambiguous
AlphaFold pLDDT
73
model confidence
Schema
Cat 4
Category 4 — Stable Fold, Function Disrupted

Clinical Evidence

ClinVar classificationUncertain significance
Review statuscriteria provided, single submitter
Associated conditions
Population frequency (gnomAD v4)Absent from gnomAD v4
cDNA changec.1585T>C
ClinVar accessionVCV004802686
Last evaluated2025/03/27 00:00

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

Full Variant Card

WFS1 Wolframin — C529R Variant Card

Molecular Atlas Pilot · RareResearch.AI · Generated by wolfram-variant-card skill

Cysteine → Arginine at position 529. Cytoplasmic loop 4. ClinVar Uncertain significance, AlphaMissense 0.519, DynaMut2 ΔΔG -0.25 kcal/mol (destabilising).


Identity

FieldValue
VariantC529R (p.Cysteine529Arginine)
DNA changec.1585T>C
Gene · ProteinWFS1 · Wolframin (890 aa)
UniProtO76024 · WFS1_HUMAN
ClinVar accessionVCV004802686
Amino acid changeCysteine (C) → Arginine (R)

Structural Context

FieldValue
AlphaFold modelAF-O76024-F1, v6
pLDDT at residue 52973.00 — well-folded
DomainCytoplasmic loop 4
Position contextLoop region · position 529 sits between transmembrane segments, solvent-accessible
IDR flagNo — pLDDT above 50 threshold

UniProt features at this position:

(none catalogued)

Position 529 sits in a connecting loop between transmembrane helices. Loop residues are typically solvent-exposed and often contribute to interhelical contacts or serve as recognition sites for binding partners. The wild-type residue is thiol (cysteine — disulfide-capable, free -SH); the mutant is positively charged (arginine — guanidinium, strong H-bond donor). The chemistry shift implies altered local packing, hydrogen-bonding, and/or electrostatics at this site.


Computational Predictions

AlphaMissense

FieldValue
am_pathogenicity0.5192
am_classambiguous
InterpretationLikely benign (threshold 0.564)

DynaMut2

FieldValue
ΔΔG (kcal/mol)-0.25 (Destabilising)
Job ID178094711327
Result URLhttps://biosig.lab.uq.edu.au/dynamut2/results_prediction/178094711327

Clinical Evidence

FieldValue
ClassificationUncertain significance
Review statuscriteria provided, single submitter
Last evaluated2025/03/27 00:00
InheritanceInheritance pattern not specified in ClinVar entry; WFS1 has both AD and AR presentations.
WFS1 variant landscapeC529R is 1 of ~326 pathogenic-spectrum variants in WFS1 (out of 2,243 catalogued in ClinVar)

(no conditions catalogued)


Research Path Decision Tree

ΔΔG < 2  + binding site affected   →  CATEGORY 3 — docking experiments
ΔΔG 2–4                            →  CATEGORY 2 — pharmacological chaperones
ΔΔG > 4                            →  CATEGORY 1 — gene therapy
pLDDT < 50                         →  CATEGORY 5 — IDR, experimental only
Stable fold + functional site hit  →  CATEGORY 4 — site-specific docking

Final Schema Categorization

Category 4 — Stable Fold, Function Disrupted

<strong>Category 4 — Stable Fold, Function Disrupted</strong><br/><br/>|ΔΔG|=0.25 negligible. Likely site-specific functional disruption — docking strategy.

Why this card matters. Wolframin's fold survives this substitution (|ΔΔG|=0.25 kcal/mol). The pathogenic signal is real — AlphaMissense places it at 0.519. Protein still folds, but a specific local site is broken. Pharmacological chaperones and small-molecule binders are the rational therapeutic vector.


Files in this folder

  • AF-O76024-F1-model_v6.pdb — AlphaFold structure
  • C529R_molstar_viewer.html — interactive 3D viewer (auto-highlights position 529 with ball-and-stick + neighbors within 5Å)
  • C529R_variant_card.md — this card (source of truth)
  • C529R_variant_card.html — styled printable card
  • C529R_dynamut2_summary.html — clean offline DynaMut2 result card
  • dynamut2_result.json — structured result data
  • dynamut2_result_page.html — local snapshot of the Biosig result page (asset URLs absolutized)
  • C529R_wildtype_interactions.pse / C529R_mutant_interactions.pse — PyMOL sessions

Generated by wolfram-variant-card skill · RareResearch.AI Molecular Atlas Every assumption documented. Every score sourced.

Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the C529R 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 C529R PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.