Fig. 1: Specialized sites within the intrinsically disordered region (IDR) of the MBD2 structure that bind NuRD complexes.
From: The role of MBD2 in immune cell development, function, and autoimmune diseases
MBD2 is composed of four domains: an N‑terminal glycine–arginine (GR) repeat region, a methyl‑CpG binding domain (MBD), an intrinsically disordered region (IDR), and a C‑terminal coiled‑coil helix. The C‑terminal helix is involved in recruitment of CHD4 and gene silencing through interaction with the NuRD subunit p66. The IDR significantly enhances DNA‑binding affinity and mediates recruitment of NuRD components RbAp48, HDAC2, and MTA2 via residues Arg286 and Leu287. Mutation of these two residues abrogates histone interactions. The figure was created on the Biorender (https://www.biorender.com/).
