Three-dimensional structure and stability of the KH domain: molecular insights 
into the fragile X syndrome

Musco, Giovanna; Stier, Gunter; Joseph, Catherine; Castiglione Morelli, Maria Antonietta; Nilges, Michael; Gibson, Toby J.; Pastore, Annalisa

doi:10.1016/S0092-8674(00)81100-9

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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome

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

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http://www.sciencedirect.com/science/article/pii/S0092867400811009/pdfft?md5=4cc2c13d5c36a61cce05261e279d5104&pid=1-s2.0-S0092867400811009-main.pdf
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Citation

Musco, G., Stier, G., Joseph, C., Castiglione Morelli, M. A., Nilges, M., Gibson, T. J., et al. (1996). Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell, 85(2), 237-245. doi:10.1016/S0092-8674(00)81100-9.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-A6DD-C

Abstract

The KH module is a sequence motif found in a number of proteins that are known to be in close association with RNA. Experimental evidence suggests a direct involvement of KH in RNA binding. The human FMR1 protein, which has two KH domains, is associated with fragile X syndrome, the most common inherited cause of mental retardation. Here we present the three−dimensional solution structure of the KH module. The domain consists of a stable beta alpha alpha beta beta alpha fold. On the basis of our results, we suggest a potential surface for RNA binding centered on the loop between the first two helices. Substitution of a well−conserved hydrophobic residue located on the second helix destroys the KH fold; a mutation of this position in FMR1 leads to an aggravated fragile X phenotype