The binding of SMRT to the deacetylase domain (HDAC3) promotes modification of chromatin structure. This process is directly related to repression of transcription.

Proceedings of the National Academy of Sciences of the United States of America
Structural insights into the interaction and activation of histone deacetylase 3 by nuclear receptor corepressors.

Solution Structure Of The Smrt Deacetylase Activation Domain

Structure Of Hdac3 Bound To Corepressor And Inositol Tetraphosphate

PREDICTED: nuclear receptor corepressor 2 isoform 4 [Macaca mulatta]

PREDICTED: nuclear receptor corepressor 2-like [Tursiops truncatus]

PREDICTED: nuclear receptor corepressor 2-like, partial [Leptonychotes weddellii]

PREDICTED: nuclear receptor corepressor 2 [Felis catus]

PREDICTED: nuclear receptor corepressor 2-like isoform X1 [Papio anubis]

TPA: nuclear receptor co-repressor 2-like [Bos taurus]

Spectrometers were equipped with 5 mm triple-resonance (1H/15N/13C) single-axis
gradient probes, and a cryoprobe for the DRX 500

the samples were degased and the tube flushed with argon