title: A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1.
abstract: The non-classical zinc finger protein, Neural Zinc Finger Factor-1, contains six Cys2His2Cys domains. All three cysteines and the second histidine directly bind Zn(II). Using a combination of mutagenesis, metal coordination and DNA binding studies, we report that the first histidine is involved in a functionally important hydrogen bonding interaction.
authors.affiliation: Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201, USA. smichel@rx.umaryland.edu.
authors.forename: Angelique N
authors.initials: AN
authors.lastname: Besold
authors.forename: Deborah L
authors.initials: DL
authors.lastname: Amick
authors.forename: Sarah L J
authors.initials: SL
authors.lastname: Michel
mesh_terms: D000818:Animals; D001665:Binding Sites; D003545:Cysteine / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism*; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism; D016335:Zinc Fingers
chemical_list: C561020:MYT1L protein, human; D009419:Nerve Tissue Proteins; D014157:Transcription Factors; D006639:Histidine; D004247:DNA; D003545:Cysteine