Journal of Molecular Biology
Volume 304, Issue 5, 15 December 2000, Pages 723-729
Journal home page for Journal of Molecular Biology

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

https://doi.org/10.1006/jmbi.2000.4308Get rights and content

Abstract

The PHD (plant homeo domain) is a ∼50-residue motif found mainly in proteins involved in eukaryotic transcription regulation. The characteristic sequence feature is a conserved Cys4-HisCys3 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 Zn2+ 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.

References (30)

Cited by (0)

Abbreviations used: DTT, dithiothreitol; TSP, 3-(trimethylsilyl)-propionate

☆☆

Edited by M. F. Summers

f1

Corresponding author

f2

E-mail address of the corresponding author: [email protected]

View full text