Fig. 7: Principal component analysis performed on backbone atoms (PCAa) of MALT1(PCASP-Ig3)339–719 models generated using AlphaFold indicates semi-independent movements of both domains pivoting around the tryptophan residue W580.
From: Insights into mechanisms of MALT1 allostery from NMR and AlphaFold dynamic analyses
a Scatter plots depict 2000 distinct conformations in the PC1 and PC2 frames, revealing the conformational heterogeneity within AF models. Conformations with outward-facing and inward-facing W580 are represented in green and orange, respectively. b, c The superposition of the two structures shown in red and blue captures the two extremes of the structural variations in the conformational ensemble along the PC1 (b) and PC2 (c) components, respectively. Arrows indicate the direction of coordinated variation between Ig3, the α1 helix, and residue W580 in MALT1(PCASP-Ig3)339–719.
