Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure

FEBS Letters
M S LeeP E Wright

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.

References

Jun 1, 1987·Biopolymers·W J Chazin, P E Wright
Sep 16, 1988·Science·G PárragaR E Klevit
Jan 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·J M Berg
Jan 15, 1988·Cell·R M Evans, S M Hollenberg
Jul 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·A D FrankelC O Pabo
Dec 16, 1983·Biochemical and Biophysical Research Communications·M RanceK Wüthrich

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Citations

Jun 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·S F MichaelJ M Berg
Sep 1, 1991·European Journal of Biochemistry·F J BlancoJ L Nieto
Apr 9, 1991·Biochemistry·R X XuR E Klevit
Jan 13, 1992·FEBS Letters·R J Mortishire-SmithP E Wright
Jan 1, 1990·Proteins·R E KlevitS J Horvath

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