2jm3
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(New page: 200px<br /><applet load="2jm3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jm3" /> '''Solution structure of the THAP domain from C...)
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Revision as of 18:53, 29 January 2008
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Solution structure of the THAP domain from C. elegans C-terminal binding protein (CtBP)
Overview
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.
About this Structure
2JM3 is a Single protein structure of sequence from Caenorhabditis elegans with as ligand. Full crystallographic information is available from OCA.
Reference
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
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