Fig. 7: Insights from integrated modelling of full-length HTT-HAP40 combining cryo-EM, SAXS and cross-linking mass spectrometry data. | Communications Biology

Fig. 7: Insights from integrated modelling of full-length HTT-HAP40 combining cryo-EM, SAXS and cross-linking mass spectrometry data.

From: Huntingtin structure is orchestrated by HAP40 and shows a polyglutamine expansion-specific interaction with exon 1

Fig. 7

a Ensemble of models for HTT-HAP40 (i) Q23 and (ii) Q54 showing only the residues defined by the cryo-EM model in surface representation (N-HEAT in blue, bridge domain in green, C-HEAT in purple and HAP40 in yellow) and exon 1-simulated residues in ribbon representation (red). b Ensemble of models for HTT-HAP40 (i) Q23, (ii) Q54 and (iii) Δexon 1 showing only the residues defined by the cryo-EM model in surface representation (N-HEAT in blue, bridge domain in green, C-HEAT in purple and HAP40 in yellow) and IDR-simulated residues in ribbon representation (grey).

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