Sequence-specific [1H]NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
Complete [1H]NMR resonance assignments are presented for the second of the three zinc fingers from SW15 as it appears in both 1- and 2-finger constructs. Signals from finger 2 are unaffected by the presence or absence of finger 1, showing that the protein has a modular construction. The structure of finger 2 comprises a helix running from N56 to Q67, and a region approximating to an anti-parallel beta-sheet running from Y42 to F53. These features combine to produce a hydrophobic core in the structure involving the invariant residues Y42, F53, L59 and H62.
Neuhaus
D
D
MRC Laboratory for Molecular Biology, Cambridge, England.
Nakaseko
Y
Y
Nagai
K
K
Klug
A
A
D000595:Amino Acid Sequence; D000818:Animals; D004268:DNA-Binding Proteins / Q000032:analysis*; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008667:Metalloproteins / Q000032:analysis*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014157:Transcription Factors; D014981:Xenopus
D004268:DNA-Binding Proteins; D008667:Metalloproteins; D014157:Transcription Factors; D006859:Hydrogen