Fig. 1: The MALT1-BCL-10 complex.
From: Insights into mechanisms of MALT1 allostery from NMR and AlphaFold dynamic analyses
a Protein domain structure: MALT1 forms a complex with the protein BCL10 through interactions between the DD and CARD domains. Sites for mono- and poly-ubiquitination are indicated. b The 4.5 Å cryo-EM model of the MALT1-BCL10 complex was created by PyMol (http://www.pymol.org/pymol) from the filament structure (PDB code 6GK2)25 reveals a filament core formed by BCL10 (blue) into which the MALT1 DD domain (orange) is inserted. Notably, none of the other domains of MALT1 are resolved in the cryo-EM study due to their high flexibility. It has been proposed that the putative arrangement of the MALT1 complex is in equilibrium between monomer and dimer forms. c MALT1 construct used within this study. d Sequence of the MALT1(PCASP-Ig3)339–719 construct, with the methyl-containing residues I, L and V labelled in blue, black and red, respectively, and the sequence covering the Ig3 domain in yellow.
