title: Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor.
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.
authors: Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd, La Jolla, CA 92037, USA.
authors: J
authors: J
authors: Pascual
authors: M
authors: M
authors: Martinez-Yamout
authors: H J
authors: HJ
authors: Dyson
authors: P E
authors: PE
authors: Wright
mesh_terms: D000595:Amino Acid Sequence; D018398:Homeodomain Proteins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism; D018980:Williams Syndrome; D015032:Zinc / Q000378:metabolism; D016335:Zinc Fingers / Q000502:physiology*
chemical_list: D018398:Homeodomain Proteins; D010446:Peptide Fragments; D014157:Transcription Factors; D015032:Zinc