Structural determinants of Cys2His2 zinc fingers

FEBS Letters

Lee, Min S.¹  Mortishire-Smith, Russell J.¹  Bolinger, Lizann²  Wright, Peter E.¹ 

[1] The Scripps Research Institute, Department of Molecular Biology, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA;University of Pennsylvania, Department of Radiology, Philadelphia, PA 19104-6021, USA

关键词: Zinc finger;    2D NMR;    Protein stability;    Supersecondary structure;    NOE;    nuclear Overhauser effect;    NOESY;    nuclear Overhauser enhancement spectroscopy;    2QF-COSY;    double quantum filtered correlation spectroscopy;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/0014-5793(92)80392-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two mutants of the zinc finger peptide Xfin-31 (Ac-YKCGLCERSFVEKSALSRHQRVHKN-CONH₂) containing alterations to the conserved hydrophobic core have been constructed and their zinc-bound structures investigated by ¹H NMR techniques. In the first (Xfin-31B) a double mutation R8F/F10G places the conserved core aromatic residue at position 8 rather than position 10. In the second (Xfin-31C), Phe-10 is replaced by Leu. A qualitative analysis of ¹H chemical shifts, NOE connectivities and coupling constants indicates that the global folds of both mutants are similar to that of the wild-type protein. However, amide exchange rates suggest that the F10L mutant is much less stable than either the wild-type or the R8F/F10G mutant.

【 授权许可】

Unknown