This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1f62
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1f62" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f62" /> '''WSTF-PHD'''<br /> ==Overview== The PHD (pl...)
Next diff →
Revision as of 14:43, 12 November 2007
|
WSTF-PHD
Overview
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.
About this Structure
1F62 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor., Pascual J, Martinez-Yamout M, Dyson HJ, Wright PE, J Mol Biol. 2000 Dec 15;304(5):723-9. PMID:11124022
Page seeded by OCA on Mon Nov 12 16:49:39 2007
