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Publication Abstract from PubMed

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.

Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP).,Liew CK, Crossley M, Mackay JP, Nicholas HR J Mol Biol. 2007 Feb 16;366(2):382-90. Epub 2006 Nov 18. PMID:17174978^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.