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PMID: 11124022 Published · ppublish English Journal Article

Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor.

Journal of molecular biology ·Vol. 304 ·No. 5 ·2000-12-15 ·Pages 723-9

Pascual J, Martinez-Yamout M, Dyson HJ, Wright PE

Abstract

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.

MeSH Terms
Amino Acid Sequence Homeodomain Proteins/chemistry,metabolism Humans Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Peptide Fragments/chemistry,metabolism Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment Sequence Homology, Amino Acid Structure-Activity Relationship Transcription Factors/chemistry,metabolism Williams Syndrome Zinc/metabolism Zinc Fingers/physiology
Chemicals
Homeodomain Proteins Peptide Fragments Transcription Factors Zinc
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Pascual J
Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd, La Jolla, CA 92037, USA.
Martinez-Yamout M
Dyson H J
Wright P E
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
2000-12-15
Pages
723-9
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Databases
PDB
SWISSPROT
Q92793
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