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XB-ART-26568
FEBS Lett 1989 Aug 28;2541-2:159-64.
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Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure.

Lee MS , Cavanagh J , Wright PE .


Abstract
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.

PubMed ID: 2506074
Article link: FEBS Lett
Grant support: [+]

Species referenced: Xenopus
Genes referenced: znf208