2JM3

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

Summary for 2JM3

• Entry DOI: 10.2210/pdb2jm3/pdb
• Descriptor: Hypothetical protein, ZINC ION (2 entities in total)
• Functional Keywords: protein, zinc finger, metal binding protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 10592.59

Authors

Liew, C.K.,Crossley, M.,Mackay, J.P.,Nicholas, H.R. (deposition date: 2006-09-21, release date: 2007-02-06, Last modification date: 2024-05-29)

Primary citation

Liew, C.K.,Crossley, M.,Mackay, J.P.,Nicholas, H.R.
Solution structure of the THAP domain from Caenorhabditis elegans C-terminal binding protein (CtBP).
J.Mol.Biol., 366:382-390, 2007

PubMed 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-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.

PubMed: 17174978
DOI: 10.1016/j.jmb.2006.11.058

Experimental method

SOLUTION NMR