Fig. 1. Schematic representation of dominant negative constructs of Xenopus laevis N-CoR. X. laevis N-CoR is a corepressor protein composed of 2498 amino acids. N-CoR can interact with nuclear hormone receptors including TR via the receptor interacting domain (ID) near the C-terminus. The repressor interacting domains (RDs) located in the N-terminal part are required for the recruitment of other corepressors such as TBL1/TBLR1 and HDAC3. The dominant negative forms, dnN-CoRs, used in this study are shown below. The myc-ID monomer comprises the ID (amino acids 1988–2349) fused to an N-terminal peptide containing myc tag and nuclear localizing sequences (NLS). The other dnN-CoR, myc-ID dimer, consists of two direct repeats of the ID separated by a linker sequence.
Image published in: Sato Y et al. (2007)
Copyright © 2007. Image reproduced with permission of the Publisher, Elsevier B. V.
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