Solution Structure of the THAP Domain from Caenorhabditis elegans C-terminal Binding Protein (CtBP). Liew, C., Crossley, M., Mackay, J., & Nicholas, H. Journal of Molecular Biology, 366(2):382-390, 2007. doi abstract bibtex 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-X2-4-Cys-X35-53-Cys-X2-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. © 2006 Elsevier Ltd. All rights reserved.
@article{
title = {Solution Structure of the THAP Domain from Caenorhabditis elegans C-terminal Binding Protein (CtBP)},
type = {article},
year = {2007},
pages = {382-390},
volume = {366},
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abstract = {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-X2-4-Cys-X35-53-Cys-X2-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. © 2006 Elsevier Ltd. All rights reserved.},
bibtype = {article},
author = {Liew, C.K. and Crossley, M. and Mackay, J.P. and Nicholas, H.R.},
doi = {10.1016/j.jmb.2006.11.058},
journal = {Journal of Molecular Biology},
number = {2}
}
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