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C529Y

Category 4 — Stable Fold, Function DisruptedUncertain significanceTransmembrane · predictedSource card
CysteineTyrosine 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 · C529Y
Mutant Y529 — energy-minimized; 3 new contacts formed
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Bond changes · DynaMut2 interaction analysis

0 lost3 gained3 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondK525K525Preserved
Hydrogen bondP533P533Preserved
Polar contactK525K525Preserved
Polar contactP533Gained
HydrophobicW371Gained
HydrophobicK525Gained

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
-0.74kcal/mol
Destabilising — mild
AlphaMissense
0.378
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 conditionsWolfram syndrome 1; Wolfram-like syndrome; Cataract 41; Autosomal dominant nonsyndromic hearing loss 6; Type 2 diabetes mellitus
Population frequency (gnomAD v4)Ultra-rare · AF 0.00034%
cDNA changec.1586G>A
ClinVar accessionVCV003892888
Last evaluated2021/07/30 00:00

Observed at very low frequency in gnomAD.

Full Variant Card

WFS1 Wolframin — C529Y Variant Card

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

Cysteine → Tyrosine at position 529. Cytoplasmic loop 4. ClinVar Uncertain significance, AlphaMissense 0.378, DynaMut2 ΔΔG -0.74 kcal/mol (destabilising).


Identity

FieldValue
VariantC529Y (p.Cysteine529Tyrosine)
DNA changec.1586G>A
Gene · ProteinWFS1 · Wolframin (890 aa)
UniProtO76024 · WFS1_HUMAN
ClinVar accessionVCV003892888
Amino acid changeCysteine (C) → Tyrosine (Y)

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 aromatic with hydroxyl (tyrosine — H-bond donor/acceptor). The chemistry shift implies altered local packing, hydrogen-bonding, and/or electrostatics at this site.


Computational Predictions

AlphaMissense

FieldValue
am_pathogenicity0.3781
am_classambiguous
InterpretationLikely benign (threshold 0.564)

DynaMut2

FieldValue
ΔΔG (kcal/mol)-0.74 (Destabilising)
Job ID178094702457
Result URLhttps://biosig.lab.uq.edu.au/dynamut2/results_prediction/178094702457

Clinical Evidence

FieldValue
ClassificationUncertain significance
Review statuscriteria provided, single submitter
Last evaluated2021/07/30 00:00
InheritanceAutosomal dominant pattern indicated by associated DFNA6/14/38 (WFS1 hearing loss 6).
WFS1 variant landscapeC529Y is 1 of ~326 pathogenic-spectrum variants in WFS1 (out of 2,243 catalogued in ClinVar)
  • Wolfram syndrome 1
  • Wolfram-like syndrome
  • Cataract 41
  • Autosomal dominant nonsyndromic hearing loss 6
  • Type 2 diabetes mellitus

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|=0.74 negligible. Likely site-specific functional disruption — docking strategy.

Why this card matters. Wolframin's fold survives this substitution (|ΔΔG|=0.74 kcal/mol). The pathogenic signal is real — AlphaMissense places it at 0.378. 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
  • C529Y_molstar_viewer.html — interactive 3D viewer (auto-highlights position 529 with ball-and-stick + neighbors within 5Å)
  • C529Y_variant_card.md — this card (source of truth)
  • C529Y_variant_card.html — styled printable card
  • C529Y_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)
  • C529Y_wildtype_interactions.pse / C529Y_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 C529Y 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 C529Y PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.