<p>The TATA-box binding protein (TBP) is required for the initiation of transcription by RNA polymerases I, II and III, from promoters with or without a TATA box [<cite idref="PUB00017043"/>, <cite idref="PUB00017042"/>]. TBP associates with a host of factors, including the general transcription factors TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core promoter. Through its association with different transcription factors, TBP can initiate transcription from different RNA polymerases. There are several related TBPs, including TBP-like (TBPL) proteins [<cite idref="PUB00017041"/>]. The C-terminal core of TBP (~180 residues) is highly conserved and contains two 77-amino acid repeats that produce a saddle-shaped structure that straddles the DNA; this region binds to the TATA box, and interacts with transcription factors and regulatory proteins [<cite idref="PUB00004136"/>].</p><p>The beta(2)-adaptor is one of four subunits that comprise the clathrin adaptor, which plays a central role in clathrin-mediated endocytosis by linking transmembrane receptors to be internalised to the clathrin lattice. The C-terminal domain of beta(2)-adaptor is the appendage or ear domain, which is involved in clathrin polymerisation.</p><p>Even though the C-terminal of beta(2)-adaptin has a very low sequence identity with the C-terminal of the TATA-box binding protein, they do share structural similarities, namely a beta-alpha-beta(4)-alpha core structure.</p> Beta2-adaptin/TATA-box binding, C-terminal