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

FEBS Letters

Lee, Min S.¹  Cavanagh, John¹  Wright, Peter E.¹ 

[1] Department of Molecular Biology, Research Institute of Scripps Clinic, 10666 North Torrey Pines Road, La Jolla, CA 920737, USA

关键词: Zinc finger;    DNA binding;    NMR;    2D;    Secondary structure;   

DOI  :  10.1016/0014-5793(89)81030-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α-helix and ending as a 3₁₀-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.

【 授权许可】

Unknown