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Figure 4
Comparison of the lateral grooves of PATZ1 and BCL6 BTB domains. The structures of the BCL6 (PDB entry 1r2b) (a) and the energy-minimized modelled mouse (b) and zebrafish (c) PATZ1 BTB domains are shown in surface representation viewed from the front and bottom. The surface area of the residues in the lateral groove of the BCL6 BTB domain is buried upon formation of the BCL6–SMRT complex (Ahmad et al., 2003BB2). The SMRT peptide binding to the BCL6 lateral groove is shown in cartoon representation in orange. All residues in the lateral groove are labelled for one monomer. Colours indicate residue type: positively charged, blue; negatively charged, red. All other residues in this region are coloured purple. The positions of the mutations that affect the binding to the co-repressor peptides in BCL6 and in PATZ1 are indicated in black (references are given in the text). A sequence alignment of BCL6 and PATZ1 BTB residues located in the lateral groove region is shown in (d). Residues are numbered according to the BCL6 and mouse PATZ1 structure files, with the charged residues coloured as in (a)–(c). Apart from positions 29 and 40, where the two alternatives are indicated, mouse and zebrafish PATZ1 contain the same residues in these structurally corresponding positions. Although the residue conservation for BCL6 and PATZ1 in this region is low, SMRT/NCOR peptides are predicted to bind the BTB domain of PATZ1 in the same region.

Journal logoSTRUCTURAL
ISSN: 2059-7983
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