BTBD6: Human BTB domain protein BDPL
PDB Code: 2VKP
The BTB domain (named after the Drosophila transcription factors Bric-a-brac, Tramtrack, and Broad) is a protein-protein interaction motif found in all eukaryotes. Sequence conservation of this motif is highly variable and widely distributed in diverse proteins. BTB domains may serve as oligomerization domains or function as binding interfaces with other proteins.
BTBD6 belongs to a BTB subfamily with a BTB-BACK-PHR domain architecture. Other members of this family including BTBD1 and BTBD2 have been shown to interact with topoisomerase 1 through the PHR domain (pfam PF08005). This C-terminal region of ~170 amino acids is predicted to represent a novel type of β-propeller structure and has sequence similarity with human protein associated with myc (PAM; NCBI accession number AAC39928), Drosophila highwire (AAF76150) and C. elegans regulator of presynaptic morphology (RPM-1; NP_505267.1).
BTBD6 expression has been found in the human lens giving rise to the alternative name “Lens BTB domain protein”.  The identified ESTs match a partial sequence previously described as “glucocorticoid receptor AF-1 coactivator-1” (AF173358) which was isolated from placenta by GST pull down.
In order to gain insight into the structure and function of BTBD6 we determined the structure of its N-terminal BTB domain at 1.6 Å resolution. This structure based on the primary swiss prot entry (Q96KE9) reveals the highly unusual deletion of the b1 and a1 elements of the dimerization interface.  These may be restored, and therefore have a potential regulatory function, in an alternative initiation site variant (gi: 119602320) which includes a further N-terminal proline rich region also present in related BTB domain proteins.

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