title: New multi zinc finger protein: biosynthetic design and characteristics of DNA recognition.
abstract: New six zinc finger protein DSp1 was created by connecting two Sp1 DNA binding domains. The DNA recognition characteristics of DSp1 demonstrate that (1) this multi finger protein binds eighteen contiguous base pairs of DNA sequence, (2) each zinc finger wraps around DNA major groove, and (3) two Sp1 domains have nonequivalent contribution to the DNA binding of DSp1.
authors.affiliation: Institute for Chemical Research, Kyoto University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Kamiuchi
authors.forename: M
authors.initials: M
authors.lastname: Imanishi
authors.forename: E
authors.initials: E
authors.lastname: Abe
authors.forename: Y
authors.initials: Y
authors.lastname: Sugiura
mesh_terms: D000595:Amino Acid Sequence; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D015202:Protein Engineering; D016329:Sp1 Transcription Factor / Q000096:biosynthesis* / Q000737:chemistry* / Q000378:metabolism; D016335:Zinc Fingers
chemical_list: D016329:Sp1 Transcription Factor; D004247:DNA