Structure of the PHD Zinc Finger from Human Williams-Beuren Syndrome Transcription Factor

• DOI: 10.1006/jmbi.2000.4308
• Publication Date: 2010-11-30T09:43:01Z
• Authors: Jaime Pascual; Maria Martinez-Ya...; H.Jane Dyson; Peter E. Wright
• Keywords: PHD finger; LIM domain; Motif (music); Sp1 transcription factor; RING finger domain; Transcription; Ring finger; Eukaryotic transcription; Structural motif; Sequence motif

The PHD (plant homeo domain) is a approximately 50-residue motif found mainly in proteins involved in eukaryotic transcription regulation. The characteristic sequence feature is a conserved Cys(4)-HisCys(3) zinc binding motif. We have determined the solution structure of the PHD motif from the human Williams-Beuren syndrome transcription factor (WSTF) protein. The domain folds into an interleaved zinc finger which binds two Zn(2+) in a similar manner to that of the RING and FYVE domains. The structure reveals a conserved zinc-binding core, together with two variable loops that are likely candidates for interactions between the various PHD domains and their specific ligands.