Towards a Molecular Understanding of the Fanconi Anemia Core Complex
Figure 2
Models of multisubunit E3 ligases. (a) A model of the proteins that make a Cullin-RING E3 ligase (CRL). The Cullin protein (lilac) acts as scaffold and binds the RING domain (cyan) required for E2 binding and the substrate binding proteins (pink, red, blue) via an adaptor. The variety of substrate binding proteins allows the CRLs flexibility in binding a range of substrates. (b) A model of the Anaphase Promoting Complex (APC). The catalytic core consists of a Cullin repeat protein Apc2 (lilac), which acts a scaffold for the RING protein, Apc11 (cyan), and the substrate binding protein Apc10 (red). For substrate recognition the APC also binds coactivators (dark blue). The APC also consists of a TPR subcomplex (green) and a platform (yellow) which orient the catalytic unit and aid binding to the co-activators. The range of subunits allows a variety of substrates to be recognised. (c) A model of the Fanconi Anemia Core Complex. The catalytic activity resides in one protein FANCL (mauve). The rest of the CC proteins are coloured blue, with light blue representing proteins associated with the CC.
