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Journal Article

The KH module has an αβ fold

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Stier,  Gunter
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Castiglione Morelli, M. A., Stier, G., Gibson, T. J., Joseph, C., Musco, G., Pastore, A., et al. (1995). The KH module has an αβ fold. FEBS Letters, 358(2), 193-198. doi:10.1016/0014-5793(94)01422-W.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-A80E-0
Abstract
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 beta 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.