Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure.
A 25-residue synthetic peptide corresponding to zinc finger 31 of the Xenopus protein Xfin adopts a compact, folded conformation in the presence of zinc. Complete 1H resonance assignments have been made. The peptide contains a helix, beginning as an alpha-helix and ending as a 3(10)-helix, that extends from residue 12 to 23. Several positively charged and polar residues located on this helix are likely to be involved in interactions with DNA. Residues 1-10 appear to adopt a hairpin-like structure.
Lee
M S
MS
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA.
Cavanagh
J
J
Wright
P E
PE
D000577:Amides / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D004268:DNA-Binding Proteins / Q000032:analysis* / Q000138:chemical synthesis; D009682:Magnetic Resonance Spectroscopy; D008667:Metalloproteins / Q000032:analysis* / Q000138:chemical synthesis; D015394:Molecular Structure; D010455:Peptides / Q000032:analysis; D011487:Protein Conformation; D014981:Xenopus; D015032:Zinc / Q000032:analysis
D000577:Amides; D004268:DNA-Binding Proteins; D008667:Metalloproteins; D010455:Peptides; D015032:Zinc