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Figure 1
Crystal structures of the BCL6 BTB domain in complex with NCoR1 BBD2 sequences. (a) The BCL6 BTB-domain dimer in complex with the low-affinity NCoR1BBD2 peptide. (b) The NCoR1BBD2-BCL6BTB chimeric protein. (c) The NCoR1BBD2 peptide interacts with two BTB-domain dimers within the crystal lattice. (d) Interfacing residues between the NCoR1BBD2 peptide and the BCL6 BTB domain. The cartoon representations in (a) and (b) depict chains of the domain-swapped BTB-domain dimer in blue and cyan and NCoR1BBD2 residues in red. The NCoR1BBD2 sequences interact with both the β1 strand and hydrophobic patch (HP) region of the BTB domain, thereby tethering two BTB dimers together. The position of the lateral groove of the BTB domain is indicated.

IUCrJ
Volume 8| Part 2| March 2021| Pages 154-160
ISSN: 2052-2525
https://doi.org/10.1107/S2052252520015754