The KH module has an αβ fold

FEBS Letters

Gibson, Toby²  Stier, Gunter²  Pastore, Annalisa²  Castiglione Morelli, Maria Antonietta¹  Travè, Gilles²  Joseph, Catherine²  Musco, Giovanna² 

[1] Università della Basilicata, Potenza, Italy;EMBL, Meyerhofstr. 1, W-69012 Heidelberg, Germany

关键词: KH;    Module;    Vigilin;    Structure;    NMR;    1D;    2D and 3D;    One-;    two- and three-dimensional;    HSQC;    heteronuclear single quantum coherence;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser enhancement;    NOESY;    2D NOE spectroscopy;    TPPI;    time-proportional phase incrementation;    TOCSY;    total correlation spectroscopy;   

DOI  :  10.1016/0014-5793(94)01422-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The KH module has recently been identified in a number of RNA associated proteins including vigilin and FMR1, a protein implicated in the fragile X syndrome. In this work, NMR spectroscopy was used to determine the secondary structure in solution of a KH domain (repeat 5 from vigilin). Almost complete assignments were obtained for the ¹H and ¹⁵N resonances using uniform ¹⁵N-labeling of the protein combined with homo-nuclear 2D ¹HNMR and 3D ¹⁵N correlated ¹H NMR. On the basis of NOE patterns, secondary chemical shifts and amide solvent exposure, the secondary structure consists of an antiparallel three stranded β sheet connected by two helical regions. This domain may also be stabilized by an appended C-terminal helix which is common to many but not all members of the KH family.

【 授权许可】

Unknown