Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP).

Chu Kong Liew, Merlin Crossley, Joel P Mackay, Hannah R Nicholas

School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales 2006, Australia. ckliew@mmb.usyd.edu.au

Journal of molecular biology 2007 Feb 16

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The THAP (Thanatos-associated protein) domain is a recently discovered zinc-binding domain found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. It contains a single zinc atom ligated by cysteine and histidine residues within a Cys-X(2-4)-Cys-X(35-53)-Cys-X(2)-His consensus. We have determined the NMR solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP) and show that it adopts a fold containing a treble clef motif, bearing similarity to the zinc finger-associated domain (ZAD) from Drosophila Grauzone. The CtBP THAP domain contains a large, positively charged surface patch and we demonstrate that this domain can bind to double-stranded DNA in an electrophoretic mobility-shift assay. These data, together with existing reports, indicate that THAP domains might exhibit a functional diversity similar to that observed for classical and GATA-type zinc fingers.

Citation

Chu Kong Liew, Merlin Crossley, Joel P Mackay, Hannah R Nicholas. Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP). Journal of molecular biology. 2007 Feb 16;366(2):382-90