Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP).
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.
Liew
Chu Kong
CK
School of Molecular and Microbial Biosciences, University of Sydney, Sydney, New South Wales 2006, Australia. ckliew@mmb.usyd.edu.au
Crossley
Merlin
M
Mackay
Joel P
JP
Nicholas
Hannah R
HR
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000502:physiology; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000502:physiology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D013329:Structure-Activity Relationship
D029742:Caenorhabditis elegans Proteins; D004268:DNA-Binding Proteins; D012996:Solutions; D000429:Alcohol Oxidoreductases; C096794:C-terminal binding protein